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The development of cancer control plans as a clearly defined concept began in the U.S. in the early 1990s. On an international level, the same concept has been described as “national cancer control planning” or national cancer control plan (NCCP) development and implementation. Recent efforts by the National Cancer Institute’s Center for Global Health and its partners have increased international and country-level interest in NCCPs. Central to the development of these plans has been a need for countries to understand the crucial factors and foundational elements necessary to develop and successfully implement a national cancer plan. This article describes the process by which a tool developed by the International Cancer Control Partnership (ICCP) helps countries and international partners assess their efforts to develop and implement a NCCP.

According to the Pan American Health Organization, noncommunicable diseases, including cancer, are the leading causes of preventable and premature death in the Americas. Governments and health care systems in Latin America face numerous challenges as a result of increasing morbidity and mortality from cancer. Multiple international organizations have recognized the need for collaborative action on and technical support for cancer research and control in Latin America. The Center for Global Health at the US National Cancer Institute (NCI-CGH) is one entity among many that are working in the region and has sought to develop a strategy for working in Latin America that draws on and expands the collaborative potential of engaged, skilled, and diverse partners. NCI-CGH has worked toward developing and implementing initiatives in collaboration with global partners that share the common objectives of building a global cancer research community and translating research results into evidence-informed policy and practice. Both objectives are complementary and synergistic and are additionally supported by an overarching strategic framework that is focused on partnerships and science diplomacy. This work highlights the overall strategy for NCI-CGH engagement in Latin America through partnerships and diplomacy, and highlights selected collaborative efforts that are aimed at improving cancer outcomes in the region.

The steady increase in cancer incidence and mortality in the Asia-Pacific presents a growing challenge to countries in the region. National cancer control planning provides key strategies for countries to decrease their cancer burden and address risk factors in the context of their populations and health systems. Evidence-guided approaches allow countries to target resources towards highly-needed and effective cancer programs, while partnerships can serve to diversify sources of support, increase coverage and sustain services. Many countries struggle to develop and implement national cancer control plans (NCCPs) due to barriers in coordinating diverse stakeholders, limited funding and absence of evidence to guide program and health infrastructure improvements. The Cancer Control Leadership Forum (CCLF) program aims to address critical hurdles in cancer control planning by: (1) convening cancer control leaders from diverse sectors; (2) raising awareness and capacity of participating country representatives to develop and implement NCCPs; (3) facilitating development of country action-plans; and (4) providing technical assistance. Two years after participating in their first CCLF, eight countries from Southeast Asia and the Pacific, represented by multiple cancer control leaders from each country, participated in an Asia-Pacific Leadership Forum Phase II (APLF2) in 2016. The APLF2 facilitated valuable experience-exchange amongst regional and international experts, and explored areas of common interest, including: improving cancer registries, strengthening training, coordinating stakeholders, maximizing resources and overcoming implementation challenges. These priorities guide on-going cancer control efforts and serve to inform the international community of trends, needs and challenges in cancer control in Southeast Asia and the Pacific.

Incorporating research objectives into national cancer control plans informs effective implementation, and ultimately, health outcomes. We sought to explore the inclusion and description of research priorities in select low- and middle-income countries’ (LMIC) cancer control plans to elucidate gaps and collaborative opportunities. LMIC plans published in English, in 2016 or later, and met World Bank and Human Development Index criteria, comprised the eligible sample. A systematic, inductive approach was used to characterize the research priorities. Two overarching categories of research priorities were identified: Establishing Research Agendas (ERA) and Building Research Capacity (BRC). Codes were subsequently assigned to distinguish between types of research and strategies for developing research capacity. Twelve LMIC cancer control plans were included in the analysis. Six of the 12 plans articulated ERA priorities involving five types of research; the most frequently planned being Health Services Research (31%), followed by Epidemiologic (27%) and Clinical (27%). Five strategies were proposed to build research capacity; the most frequently proposed were “Enhance Cancer Surveillance” (44%) and “Establish Research Infrastructure” (24%). Country-specific variation in ERA and BRC priorities were observed across research type and cancer continuum phase. This is the first systematic examination of research priorities in a subset of LMIC national cancer control plans. Findings suggest that some LMICs intend to focus their research efforts in specific areas and others plan to integrate research across the continuum to enhance cancer control efforts. The extent and overlap of research priorities between countries demonstrates promise for trans-national research collaborations.

Background: There is increasing demand for dissemination and implementation of evidence-based guidelines in cancer control. In 2017, the National Cancer Institute's Center for Global Health (NCI-CGH) partnered with University of New Mexico and The University of Texas MD Anderson Cancer Center to provide the Project ECHO (Extension for Community Healthcare Outcomes) model of tele-mentoring as an extension of existing programs that convene relevant stakeholders for knowledge sharing and technical assistance in national cancer control planning. In early 2018, NCI-CGH launched Project ECHO programs in the Caribbean, Asia-Pacific, and sub-Saharan Africa regions, and began plans for implementation in south Asia. As a new approach for the center in program development, NCI-CGH included evaluation measures from the inception of the program to adequately measure its efficacy. Aim: Evaluation of NCI-CGH Project ECHO programs will guide future program development, and assess achievement of the program's goals: (1) to increase individual participant knowledge in specific areas; (2) to improve application of the knowledge learned; and (3) to increase collaboration within and among countries. Methods: Using Project ECHO Evaluation 101, a guide developed by the New York Academy of Medicine, NCI-CGH developed a comprehensive logic model including a concise list of program outcomes prior to the launch of ECHO programs. NCI-CGH used the logic model to develop and pilot-test a Web-based baseline and post-ECHO survey, to be completed by participants in each program, that measures participants' knowledge of cancer control planning principles and strategies. NCI-CGH conducted the baseline survey for all three ECHO programs. The post-ECHO survey will be distributed at the conclusion of each program. Each program is expected to run for approximately six months to one year. Results: Response rates for baseline surveys were: 32% in the Caribbean, 43% in Asia-Pacific, and 78% in sub-Saharan Africa. Respondents (by region) reported high levels of knowledge of the following evidence-based principles and guidelines: the Caribbean - HPV vaccination, Asia-Pacific - cervical cancer early diagnosis, sub-Saharan Africa - raising awareness. Low levels of knowledge were reported for: psychosocial support for cancer patients, family members, and caregivers in the Caribbean; survivorship care for cancer patients in Asia-Pacific; and alcohol consumption control in sub-Saharan Africa. This presentation will highlight baseline and post-ECHO survey analysis findings and the impact of these data on future program development. Conclusion: Inclusion of evaluation measures in the design phase of NCI-CGH Project ECHO tele-mentoring programs enhanced planning efforts by providing a blueprint for developing program curricula, creating an embedded system for gathering data from participants, and informing the pathway to future improvements.

Background: The Cancer Resolution approved at the 2017 World Health Assembly highlighted the need to improve the evidence base for cancer prevention and control through research. Research priorities articulated in national cancer control plans can promote effective cancer control, especially in low and middle-income countries (LMIC) that bear a significant cancer burden and where local research is scarce. Understanding how LMICs address research in their cancer control plans may enhance integration of research and control efforts. Aim: We sought to systematically identify and characterize the research priorities in select LMIC cancer control plans. Methods: LMIC plans published in English and in 2016 or later, that met World Bank and Human Development Index criteria and were identified. Key terms were used to identify relevant research-related content. A systematic, inductive approach was used to examine for clusters of concepts or topics, and codes were applied to characterize the research priorities into categories, phases, types, dimensions and aspects. Results: A total of 12 LMIC plans were deemed to be eligible for the analysis. Two overarching categories of research-related content were identified: Establishing a Research Agenda (ERA), where specific types and topics of research were articulated, and Building Research Capacity (BRC), for content describing intention to plan or facilitate research. Six LMICs included a total of 67 ERA priorities involving five types of research. Health Services Research was the most frequently reported type of research (31%). The research topics in the treatment/management phase were most frequently identified (30%). Three of the six countries had the most number of ERA research priorities. A total of 126 BRC priorities were identified across five dimensions. Two BRC dimensions were most frequently proposed: Enhance Cancer Surveillance (44%) and Establish Research Infrastructure (24%), and subsequent aspect codes elucidated a range of activities. Five aspects characterized focal areas in cancer surveillance while two aspects revealed focal areas for research infrastructure. Country-specific variation in ERA and BRC priorities were seen. Priorities were mapped to illustrate the breadth and depth of research priorities in LMICs' plans. Details of the distribution of research by country and by dimensions will be discussed. Conclusion: This first comprehensive examination of research priorities in LMIC cancer plans revealed countries' commitment to incorporate research into their cancer control efforts. The extent of research-related priorities demonstrates promise for transnational research collaborations. Next steps include improved understanding of key factors in achieving successful integration of research and control efforts through cancer control plan implementation.

The phosphoserine/threonine binding protein 14-3-3 stimulates the catalytic activity of protein kinase C-epsilon (PKCepsilon) by engaging two tandem phosphoserine-containing motifs located between the PKCepsilon regulatory and catalytic domains (V3 region). Interaction between 14-3-3 and this region of PKCepsilon is essential for the completion of cytokinesis. Here, we report the crystal structure of 14-3-3zeta bound to a synthetic diphosphorylated PKCepsilon V3 region revealing how a consensus 14-3-3 site and a divergent 14-3-3 site cooperate to bind to 14-3-3 and so activate PKCepsilon. Thermodynamic data show a markedly enhanced binding affinity for two-site phosphopeptides over single-site 14-3-3 binding motifs and identifies Ser 368 as a gatekeeper phosphorylation site in this physiologically relevant 14-3-3 ligand. This dual-site intra-chain recognition has implications for other 14-3-3 targets, which seem to have only a single 14-3-3 motif, as other lower affinity and cryptic 14-3-3 gatekeeper sites might exist.

ZiPD (zinc phosphodiesterase; synonyms are ElaC, ecoZ, RNaseZ and 3' tRNase) and the iron-dependent redox enzyme FlRd (flavorubredoxin) from Escherichia coli represent prototypical cases of proteins sharing the metallo-beta-lactamase fold that require strict metal selectivity for catalytic activity, yet their metal selectivity has only been partially understood. In contrast with hydrolytic metallo-beta-lactamase proteins, iron-dependent FlRd-like enzymes have an atypical glutamate ligand, which replaces one otherwise conserved histidine ligand. X-ray absorption spectroscopy revealed that the FlRd metallo-beta-lactamase domain is capable of incorporating two zinc ions into the binuclear metal-binding site. Zinc dissociation constants, determined by isothermal titration calorimetry are similar for zinc binding to E. coli ZiPD (K(d1)=2.2+/-0.2 microM and K(d2)=23.0+/-0.6 microM) and to the E. coli FlRd metallo-beta-lactamase domain (K(d1)=0.7+/-0.1 microM and K(d2)=26.0+/-0.1 microM). In good correspondence, apo-ZiPD requires incubation with 10 microM zinc for full reconstitution of the phosphodiesterase activity. Accordingly, metal selectivity of ZiPD and FlRd only partially relies on first shell metal ligands. Back mutation of the atypical glutamate in FlRd to a histidine unexpectedly resulted in an increased first zinc dissociation constant (K(d1)=30+/-4 microM and K(d2)=23+/-2 microM). In combination with a recent mutational study on ZiPD [Vogel, Schilling and Meyer-Klaucke (2004) Biochemistry 43, 10379-10386], we conclude that the atypical glutamate does not guide metal selectivity of the FlRd metallo-beta-lactamase domain but suppresses possible hydrolytic cross-activity.

Abstract 61 Background: In May 2015, the US National Cancer Institute, Center for Global Health (NCI/CGH) partnered with the American Cancer Society and the Healthy Caribbean Coalition to convene the Caribbean Cancer Control Leadership Forum (CCLF), with participating teams from five Caribbean countries: Bahamas, Barbados, Belize, Jamaica, and Trinidad and Tobago. The CCLF also included country representatives from Antigua, Dominica, Haiti, St Maarten, and Suriname. NCI/CGH convenes a regional CCLF to increase the capacity of participating countries to initiate or enhance cancer control planning and implementation. Country teams include four to six cancer control leaders, each of whom can positively influence their country’s ability to develop and implement a national cancer control plan (NCCP). Since 2015, several country teams have made substantive progress on their action plans and have continued communication with NCI/CGH and its partner, and other countries in the region have taken important steps toward developing NCCPs. NCI/CGH has recognized the utility in reconvening the country teams to further advance their cancer control planning goals, while providing additional technical assistance, mentorship, and networking opportunities. In May 2017, NCI/CGH and partners will host a 2-day phase II Caribbean CCLF as an opportunity for country teams to share progress and challenges, identify solutions, advance action related to development and implementation of NCCP, build country successes, and promote regional control partnership and collaboration via interactive panel sessions, roundtables, and action planning. Methods: The phase II CCLF will include four pre-CCLF webinars, information sharing discussions, adequate team preparation, and in-person interactive sessions and roundtables. Potential topics include: using cancer program toolkits and other data for decision-making; moving from pilot to scale-up phase for cervical cancer prevention and screening programs; and methods to develop registry and pathology infrastructure. Results and Conclusion: With this phase II CCLF, we are targeting the following outcomes: expanded knowledge of NCCP concepts tailored to an individual country’s needs; enhanced and attainable action plans to move forward the NCCP at the country level; and enriched regional collaboration between countries to overcome potential future planning challenges. AUTHORS' DISCLOSURES OF POTENTIAL CONFLICTS OF INTEREST No COIs from the authors.

Summary Atypical protein kinase C (aPKC) is a key apical-basal polarity determinant and Par complex component. It is recruited by Par3/Baz (Bazooka in Drosophila) into epithelial apical domains through high-affinity interaction. Paradoxically, aPKC also phosphorylates Par3/Baz, provoking its relocalization to adherens junctions (AJs). We show that Par3 conserved region 3 (CR3) forms a tight inhibitory complex with a primed aPKC kinase domain, blocking substrate access. A CR3 motif flanking its PKC consensus site disrupts the aPKC kinase N lobe, separating P-loop/αB/αC contacts. A second CR3 motif provides a high-affinity anchor. Mutation of either motif switches CR3 to an efficient in vitro substrate by exposing its phospho-acceptor site. In vivo, mutation of either CR3 motif alters Par3/Baz localization from apical to AJs. Our results reveal how Par3/Baz CR3 can antagonize aPKC in stable apical Par complexes and suggests that modulation of CR3 inhibitory arms or opposing aPKC pockets would perturb the interaction, promoting Par3/Baz phosphorylation., Graphical Abstract, Highlights • Sequences flanking the Par3 CR3 consensus PKC site cooperate to inhibit aPKC • A Par3 CR3 inhibitory arm disrupts aPKC P-loop/αB/αC contacts and αC-helix position • Mutating either CR3 arm switches Par3 into an efficient aPKC substrate in vitro • Equivalent Bazooka substitutions alter its apical localization to AJs in vivo, Par3 is required for aPKC membrane recruitment, yet it polarizes to adherens junctions upon phosphorylation. Soriano et al. show that Par3 antagonizes active aPKC kinase by separating crucial N-lobe contacts. Disrupting high-affinity Par3 contacts switches it to an efficient aPKC substrate and polarizes Par3/Bazooka from apical domains to adherens junctions.

The aPKC [atypical PKC (protein kinase C)] isoforms ι and ζ play crucial roles in the formation and maintenance of cell polarity and represent attractive anti-oncogenic drug targets in Ras-dependent tumours. To date, few isoform-specific chemical biology tools are available to inhibit aPKC catalytic activity. In the present paper, we describe the identification and functional characterization of potent and selective thieno[2,3-d]pyrimidine-based chemical inhibitors of aPKCs. A crystal structure of human PKCι kinase domain bound to a representative compound, CRT0066854, reveals the basis for potent and selective chemical inhibition. Furthermore, CRT0066854 displaces a crucial Asn-Phe-Asp motif that is part of the adenosine-binding pocket and engages an acidic patch used by arginine-rich PKC substrates. We show that CRT0066854 inhibits the LLGL2 (lethal giant larvae 2) phosphorylation in cell lines and exhibits phenotypic effects in a range of cell-based assays. We conclude that this compound can be used as a chemical tool to modulate aPKC activity in vitro and in vivo and may guide the search for further aPKC-selective inhibitors.

43 A National Cancer Control Plan (NCCP) comprises an important part of a country’s non-communicable disease (NCD) plan and can help countries meet NCD targets outlined in the WHO Global NCD Action Plan. A comprehensive cancer control plan is based on data such as a country’s cancer burden and cancer risk factors, available resources, and local context of culture and health care. The plan provides a systematic framework for implementation of evidence-based and cost-effective strategies for cancer prevention and control. The InternationalCancerControl LeadershipForum isa2-3day regionalworkshopwith thematic seminar modules on cancer control planning and implementation, aswell as interactive action planning sessions. The goal is to increase the capacity of participating countries to initiate or enhance cancer control planning and implementation through a multisectoral approach. The country teams are composed of high-level leaders who represent government agencies, civil society, oncology professionals, and academia. The program approach engages country teams over a year and a half. Approximately 3-6months prior to the forum, teams conduct a situational analysis of the cancer burden and cancer control planning efforts in their country. During the Forum, teams are introduced to evidence-based approaches and exchange best-practices with colleagues to develop a 12-month action plan to move their cancer control planning and implementation efforts forward. In the year after the Forum, country teams and Forum faculty meet for 3-4 follow-upphone calls to address technical assistanceneeds as countries begin to implement their actionplan.Thus far, Forumshavebeenheld inAfrica,SoutheastAsia, thePacific, theCaribbean,Middle East-North Africa, Latin America, and Central Asia regions. The country teams report that the Forum provides an important opportunity to plan with diverse stakeholders. Participants also report increased awareness and knowledge on developing and implementing a national cancer control plan, and learn best-practices from their colleagues in neighboring countries. In some Forums, countries have shown interest to work collaboratively towards regional initiatives. AUTHORS’ DISCLOSURES OF POTENTIAL CONFLICTS OF INTEREST: No COIs from the authors. Tulika Singh,BrendaKostelecky, and Lisa Stevens, Center forGlobalHealth,National Cancer Institute (NCI),National Institutes of Health, US Department of Health and Human Services Corresponding author: Brenda Kostelecky, Center for Global Health, National Cancer Institute (NCI), National Institutes of Health, US Department of Health and Human Services, 9609 Medical Center Dr, Rockville, MD 20852; 240-276-5585; kosteleckybd@mail.nih.gov DOI: 10.1200/JGO.2016.004853 Tulika Singh Brenda Kostelecky

Mitochondria are highly dynamic organelles that mediate essential cell functions such as apoptosis and cell-cycle control in addition to their role as efficient ATP generators. Mitochondrial morphology changes are tightly regulated, and their shape can shift between small, fragmented units and larger networks of elongated mitochondria. We demonstrate that mitochondrial elements become significantly elongated and interconnected shortly after nutrient depletion. This mitochondrial morphological shift depends on the type of starvation, with an additive effect observed when multiple nutrients are depleted simultaneously. We further show that starvation-induced mitochondrial elongation is mediated by down-regulation of dynamin-related protein 1 (Drp1) through modulation of two Drp1 phosphorylation sites, leading to unopposed mitochondrial fusion. Finally, we establish that mitochondrial tubulation upon nutrient deprivation protects mitochondria from autophagosomal degradation, which could permit mitochondria to maximize energy production and supply autophagosomal membranes during starvation.

Mitochondria continuously change their shape and thereby influence different cellular processes like cell death or development. Recently, we showed that during starvation mitochondria fuse into a highly connected network. The change in mitochondrial shape was dependent on inactivation of the fission protein Drp1, through targeting of two different phosphorylation sites. This rapid inhibition of mitochondrial fission led to unopposed fusion, protecting mitochondria from starvation-induced degradation and enabling the cell to survive nutrient scarce conditions.

Protein kinase C epsilon (PKCe) priming involves phosphorylation of the kinase domain at 3 different sites. Whether these phosphorylation events were autocatalytic was unclear. Now Parker and colleagues use different PKCe mutants and inhibitors to demonstrate that the occupancy of the nucleotide binding pocket, and not catalytic activity, promote priming of PKCe. The protein kinase C (PKC) Ser/Thr kinases account for ∼2% of the human kinome and regulate diverse cellular behaviors. PKC catalytic activity requires priming phosphorylations at three conserved sites within the kinase domain. Here we demonstrate that priming of PKC is dependent on the conformation of the nucleotide binding pocket but not on its intrinsic kinase activity. Inactive ATP binding site mutants are unprimed, but they become phosphorylated upon occupancy of the ATP binding pocket with inhibitors of PKC. We have exploited this property to screen for PKC inhibitors in vivo. Further, we generated a distinct class of kinase-inactive mutants that maintain the integrity of the ATP binding pocket; such mutants are constitutively primed and functionally distinct from ATP binding site mutants. These data demonstrate that autophosphorylation is not required for PKC priming and show how ATP pocket occupation can enable a kinase to mature as well as function.

The PKB (protein kinase B) and PKC (protein kinase C) families display highly related catalytic domains that require a largely conserved series of phosphorylations for the expression of their optimum activities. However, in cells, the dynamics of these modifications are quite distinct. Based on experimental evidence, it is argued that the underlying mechanisms determining these divergent behaviours relate to the very different manner in which their variant regulatory domains interact with their respective catalytic domains. It is concluded that the distinct behaviours of PKB and PKC proteins are defined by the typical ground states of these proteins.

The elaC gene product from Escherichia coli , ZiPD, is a 3′ tRNA-processing endonuclease belonging to the tRNase Z family of enzymes that have been identified in a wide variety of organisms. In contrast to the elaC homologue from Bacillus subtilis , E. coli elaC is not essential for viability, and although both enzymes process only precursor tRNA (pre-tRNA) lacking a CCA triplet at the 3′ end in vitro, the physiological role of ZiPD remains enigmatic because all pre-tRNA species in E. coli are transcribed with the CCA triplet. We present the first crystal structure of ZiPD determined by multiple anomalous diffraction at a resolution of 2.9 Å. This structure shares many features with the tRNase Z enzymes from B. subtilis and Thermotoga maritima , but there are distinct differences in metal binding and overall domain organization. Unlike the previously described homologous structures, ZiPD dimers display crystallographic symmetry and fully loaded metal sites. The ZiPD exosite is similar to that of the B. subtilis enzyme structurally, but its position with respect to the protein core differs substantially, illustrating its ability to act as a clamp in binding tRNA. Furthermore, the ZiPD crystal structure presented here provides insight into the enzyme's cooperativity and assists the ongoing attempt to elucidate the physiological function of this protein.

Escherichia coli ZiPD is the best characterized protein encoded by the elaC gene family and is a model for the 3'-pre-tRNA processing endoribonucleases (tRNase Z). A metal ligand-based sequence alignment of ZiPD with metallo-beta-lactamase domain proteins of known crystallographic structure identifies a ZiPD-specific sequence insertion of approximately 50 residues, which we will refer to as the ZiPD exosite. Functionally characterized ZiPD homologs from Bacillus subtilis, Methanococcus janaschii, and human share the presence of the ZiPD exosite, which is also present in the amino-terminal, but not in the carboxyl-terminal, domain of ElaC2 proteins. Another class of functionally characterized tRNase Z enzymes from Thermotoga maritima and Arabidopsis thaliana lack characteristic motifs in the exosite but possess a sequence segment with clustered basic amino acid residues. As an experimental attempt to investigate the function of the exosite we constructed a ZiPD variant that lacks this module (ZiPDDelta). ZiPDDelta has almost wild-type-like catalytic properties for hydrolysis of the small, chromogenic substrate bis(p-nitrophenyl) phosphate. Removal of the ZiPD exosite only affects k(cat), which is reduced by less than 40%, whereas both K' andthe Hill coefficient (measures of the substrate affinity and cooperativity, respectively) remain unchanged. Hence, the exosite is not required for the intrinsic phosphodiesterase activity of ZiPD. Removal of the exosite also does not affect the dimerization properties of ZiPD. In contrast to the wild-type enzyme, ZiPDDelta does not process pre-tRNA, and gel shift assays demonstrate that only the wild-type enzyme, but not ZiPDDelta, binds mature tRNA. These findings show that the exosite is essential for pre-tRNA recognition. In conclusion, we identify a ZiPD exosite that guides physiological substrate recognition in the ZiPD/ElaC protein family.

Infectious Agents and Cancer is introducing a new section on Cancer Centers in Low- and Middle-Income Countries intended to provide the oncology community with detailed information about lessons learned in cancer control in resource-limited settings. The growing burden of cancer and the high rates of infection-related cancers in Low- and Middle-Income Countries (LMICs) argue for exploring the successes and challenges of cancer centers in low-resource settings. Detailed analyses are needed on how successful cancer centers have developed and managed such key components as strategic partnerships, trained cancer professionals, sustainable funding, appropriate technology, and research capacity. Many examples exist wherein local cancer centers have made significant progress and as such, the series will provide a platform to showcase detailed features of cancer institutes in LMICs and provide valuable information for those seeking to replicate successful models and to help invigorate efforts to build cancer capacity.