PEBP1/RKIP behavior: a mirror of actin-membrane organization
Autor: | Slavica Jonic, Françoise Schoentgen |
---|---|
Přispěvatelé: | Institut de minéralogie, de physique des matériaux et de cosmochimie (IMPMC), Muséum national d'Histoire naturelle (MNHN)-Institut de recherche pour le développement [IRD] : UR206-Sorbonne Université (SU)-Centre National de la Recherche Scientifique (CNRS) |
Rok vydání: | 2019 |
Předmět: |
rho GTP-Binding Proteins
MAP Kinase Signaling System Cell Motility Phosphatidylethanolamine Binding Protein GTPase [SDV.BC.BC]Life Sciences [q-bio]/Cellular Biology/Subcellular Processes [q-bio.SC] Biology cell shape 03 medical and health sciences Cellular and Molecular Neuroscience Downregulation and upregulation Membrane organization medicine Humans Amino Acid Sequence Cytoskeleton Molecular Biology membrane Actin Pharmacology 0303 health sciences Kinase 030302 biochemistry & molecular biology Cell Membrane cytoskeleton [SDV.BBM.BM]Life Sciences [q-bio]/Biochemistry Molecular Biology/Molecular biology Cell Biology Actins Cell biology medicine.anatomical_structure motility rab GTP-Binding Proteins Molecular Medicine actin |
Zdroj: | Cellular and Molecular Life Sciences Cellular and Molecular Life Sciences, 2020, 77 (5), pp.859-874. ⟨10.1007/s00018-020-03455-5⟩ Cellular and Molecular Life Sciences, Springer Verlag, 2020, 77 (5), pp.859-874. ⟨10.1007/s00018-020-03455-5⟩ |
ISSN: | 1420-9071 1420-682X |
DOI: | 10.1007/s00018-020-03455-5⟩ |
Popis: | International audience; Phosphatidylethanolamine binding protein 1 (PEBP1), a small 21kDa protein, is implicated in several key processes of the living cell. The deregulation of PEBP1, especially its downregulation, leads to major diseases such as cancer and Alzheimer's disease. PEBP1 was found to interact with numerous proteins, especially kinases and GTPases, generally inhibiting their activity. To understand the basic functionality of this amazing small protein, we have considered several known processes it modulates and we have discussed the role of each molecular target in these processes. Here, we propose that cortical actin organization, associated with membrane changes, is involved in the majority of the processes modulated by PEBP1. Furthermore, based on recent data, we summarize some key PEBP1-interacting proteins, we report their respective functions and focus on their relationships with actin organization. We suggest that, depending on the cell status and environment, PEBP1 is an organizer of the actin-membrane composite material. |
Databáze: | OpenAIRE |
Externí odkaz: |