Search

Your search keyword '"Lutz, Pierre G."' showing total 35 results
Start Over Author "Lutz, Pierre G."
35 results on '"Lutz, Pierre G."'

10. Molecular Tuning of Filamin A Activities in the Context of Adhesion and Migration

Author

Lamsoul, Isabelle, Dupré, Loïc, Lutz, Pierre G., Centre de Physiopathologie Toulouse Purpan (CPTP), Université Toulouse III - Paul Sabatier (UT3), Université Fédérale Toulouse Midi-Pyrénées-Université Fédérale Toulouse Midi-Pyrénées-Institut National de la Santé et de la Recherche Médicale (INSERM)-Centre National de la Recherche Scientifique (CNRS), and Lutz, Pierre

Subjects
[SDV] Life Sciences [q-bio], Cell and Developmental Biology, animal structures, actin cytoskeleton, cell migration, integrin, Mini Review, [SDV]Life Sciences [q-bio], cell adhesion, Cell Biology, macromolecular substances, filamin, Developmental Biology
Abstract

International audience; The dynamic organization of actin cytoskeleton meshworks relies on multiple actinbinding proteins endowed with distinct actin-remodeling activities. Filamin A is a large multi-domain scaffolding protein that cross-links actin filaments with orthogonal orientation in response to various stimuli. As such it plays key roles in the modulation of cell shape, cell motility, and differentiation throughout development and adult life. The essentiality and complexity of Filamin A is highlighted by mutations that lead to a variety of severe human disorders affecting multiple organs. One of the most conserved activity of Filamin A is to bridge the actin cytoskeleton to integrins, thereby maintaining the later in an inactive state. We here review the numerous mechanisms cells have developed to adjust Filamin A content and activity and focus on the function of Filamin A as a gatekeeper to integrin activation and associated adhesion and motility.

Published
2020

13. JAM-L-mediated leukocyte adhesion to endothelial cells is regulated in cis by [alpha]4[beta]1 integrin activation

Author

Luissint, Anny-Claude, Lutz, Pierre G., Calderwood, David A., Couraud, Pierre-Olivier, and Bourdoulous, Sandrine

Subjects
Cell adhesion molecules -- Chemical properties, Cell adhesion -- Research, Endothelium -- Chemical properties, Biological sciences
Abstract

Junctional adhesion molecules (JAMs) are endothelial and epithelial adhesion molecules involved in the recruitment of circulating leukocytes to inflammatory sites. We show here that JAM-L, a protein related to the JAM family, is restricted to leukocytes and promotes their adhesion to endothelial cells. Cis dimerization of JAM-L is required to engage in heterophilic interactions with its cognate counter-receptor CAR (cox-sackie and adenovirus receptor). Interestingly, JAM-L expressed on neutrophils binds CAR independently of integrin activation. However, on resting monocytes and T lymphocytes, which express the integrin VLA-4, JAM-L molecules engage in complexes with VLA-4 and mainly accumulate in their monomeric form. Integrin activation is required for the dissociation of JAM-L-VLA-4 complexes and the accumulation of functional JAM-L dimers, which indicates that the leukocyte integrin VLA-4 controls JAM-L function in cis by controlling its dimerization state. This provides a mechanism through which VLA-4 and JAM-L functions are coordinately regulated, allowing JAM-L to strengthen integrin-dependent adhesion of leukocytes to endothelial cells.

Published
2008

32. PRAM-1 Is a Novel Adaptor Protein Regulated by Retinoic Acid (RA) and Promyelocytic Leukemia (PML)-RA Receptor α in Acute Promyelocytic Leukemia Cells

Author

Moog-Lutz, Christel, primary, Peterson, Erik J., additional, Lutz, Pierre G., additional, Eliason, Steve, additional, Cavé-Riant, Florence, additional, Singer, Andrew, additional, Di Gioia, Yolande, additional, Dmowski, Sally, additional, Kamens, Joanne, additional, Cayre, Yvon E., additional, and Koretzky, Gary, additional

Published
2001
Full Text
View/download PDF

34. PRAM-i Potentiates Arsenic Trioxide-induced JNK Activation.

Author

Denis, Frédéric M., Benecke, Arndt, Di Gioia, Yolande, Touw, Ivo P., Cayre, Yvon E., and Lutz, Pierre G.

Subjects
*MYELOID leukemia, *LEUKEMIA, *TRETINOIN, *GENE expression, *ONCOLOGY, *BIOCHEMISTRY
Abstract

The promyelocytic leukemia RARα target gene encoding an adaptor molecule-1 (PRAM-1) is involved in a signaling pathway induced by retinoic acid in acute promyelocytic leukemia (APL) cells. To better understand the function of PRAM-1, we have undertaken the identification of its partners through a yeast two-hybrid screen. Here, we show that the proline-rich domain of PRAM-1 interacted with the Src homology 3 (SH3) domain of hematopoietic progenitor kinase 1 (HPK-1)-interacting protein of 55 kDa (HIP-55, also called SH3P7 and Abp1) known to stimulate the activity of HPK-1 and c-Jun N-terminal kinase (JNK). Overexpression of PRAM-1 in the NB4 APL cell line increased arsenic trioxide-induced JNK activation through a caspase 3-like-dependent activity. Dissociation of the SH3 domain from the rest of the HIP-55 protein was observed in the NB4 APL cell line treated with arsenic trioxide due to specific cleavage by caspase 3-like enzymes. The cleavage of HIP-55 correlated with the induction of PRAM-1 mRNA and protein expression. Taken together, our results suggest that the caspase 3-cleaved SH3 domain of HIP-55 is likely involved in PRAM-1-mediated JNK activation upon arsenic trioxide-induced differentiation of NB4 cells. [ABSTRACT FROM AUTHOR]

Published
2005
Full Text
View/download PDF

35. Molecular Tuning of Filamin A Activities in the Context of Adhesion and Migration.

Author

Lamsoul I, Dupré L, and Lutz PG

Abstract

The dynamic organization of actin cytoskeleton meshworks relies on multiple actin-binding proteins endowed with distinct actin-remodeling activities. Filamin A is a large multi-domain scaffolding protein that cross-links actin filaments with orthogonal orientation in response to various stimuli. As such it plays key roles in the modulation of cell shape, cell motility, and differentiation throughout development and adult life. The essentiality and complexity of Filamin A is highlighted by mutations that lead to a variety of severe human disorders affecting multiple organs. One of the most conserved activity of Filamin A is to bridge the actin cytoskeleton to integrins, thereby maintaining the later in an inactive state. We here review the numerous mechanisms cells have developed to adjust Filamin A content and activity and focus on the function of Filamin A as a gatekeeper to integrin activation and associated adhesion and motility., (Copyright © 2020 Lamsoul, Dupré and Lutz.)

Published
2020
Full Text
View/download PDF

Catalog

Books, media, physical & digital resources
See catalog results