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1 H, 13 C, and 15 N assignments of the mRNA binding protein hnRNP A18.
- Source :
-
Biomolecular NMR assignments [Biomol NMR Assign] 2023 Jun; Vol. 17 (1), pp. 37-41. Date of Electronic Publication: 2022 Dec 21. - Publication Year :
- 2023
-
Abstract
- Heterogeneous ribonuclear protein A18 (hnRNP A18) is an RNA binding protein (RBP) involved in the hypoxic cellular stress response and regulation of cytotoxic T-lymphocyte-associated protein 4 (CTLA-4) expression in melanoma, breast cancer, prostate cancer, and colon cancer solid tumors. hnRNP A18 is comprised of an N-terminal structured RNA recognition motif (RMM) and a C-terminal intrinsically disordered domain (IDD). Upon cellar stressors, such as UV and hypoxia, hnRNP A18 is phosphorylated by casein kinase 2 (CK2) and glycogen synthase kinase 3β (GSK-3β). After phosphorylation, hnRNP A18 translocates from the nucleus to the cytosol where it interacts with pro-survival mRNA transcripts for proteins such as hypoxia inducible factor 1α and CTLA-4. Both the hypoxic cellular response and modulation of immune checkpoints by cancer cells promote chemoradiation resistance and metastasis. In this study, the <superscript>1</superscript>  H, <superscript>13</superscript>  C, and <superscript>15</superscript>  N backbone and sidechain resonances of the 172 amino acid hnRNP A18 were assigned sequence-specifically and provide a framework for future NMR-based drug discovery studies toward targeting hnRNP A18. These data will also enable the investigation of the dynamic structural changes within the IDD of hnRNP A18 upon phosphorylation by CK2 and GSK-3β to provide critical insight into the structure and function of IDDs.<br /> (© 2022. The Author(s).)
- Subjects :
- Male
Humans
RNA, Messenger metabolism
Glycogen Synthase Kinase 3 beta metabolism
CTLA-4 Antigen metabolism
Nuclear Magnetic Resonance, Biomolecular
Protein Binding
Carrier Proteins metabolism
Heterogeneous-Nuclear Ribonucleoproteins genetics
Heterogeneous-Nuclear Ribonucleoproteins metabolism
Subjects
Details
- Language :
- English
- ISSN :
- 1874-270X
- Volume :
- 17
- Issue :
- 1
- Database :
- MEDLINE
- Journal :
- Biomolecular NMR assignments
- Publication Type :
- Academic Journal
- Accession number :
- 36539586
- Full Text :
- https://doi.org/10.1007/s12104-022-10117-z