Focal adhesion kinase-dependent activation of the early endocytic protein Rab5 is associated with cell migration.

PTK2 protein tyrosine kinase 2 (PTK2) Rab5 cell migration early endosome endocytic trafficking focal adhesion focal adhesion kinase (FAK) integrin complex metastasis small GTPase tumor

Journal

The Journal of biological chemistry
ISSN: 1083-351X
Titre abrégé: J Biol Chem
Pays: United States
ID NLM: 2985121R

Informations de publication

Date de publication:
23 08 2019
Historique:
received: 01 04 2019
revised: 17 06 2019
pubmed: 12 7 2019
medline: 31 3 2020
entrez: 12 7 2019
Statut: ppublish

Résumé

Focal adhesion kinase (FAK) is a central regulator of integrin-dependent cell adhesion and migration and has recently been shown to co-localize with endosomal proteins. The early endocytic protein Rab5 controls integrin trafficking, focal adhesion disassembly, and cell migration and has been shown to be activated upon integrin engagement by mechanisms that remain unclear. Because FAK is a critical regulator of integrin-dependent signaling and Rab5 recapitulates FAK-mediated effects, we evaluated the possibility that FAK activates Rab5 and contributes to cell migration. Pulldown assays revealed that Rab5-GTP levels are decreased upon treatment with a pharmacological inhibitor of FAK, PF562,271, in resting A549 cells. These events were associated with decreased peripheral Rab5 puncta and a reduced number of early endosome antigen 1 (EEA1)-positive early endosomes. Accordingly, as indicated by FAK inhibition experiments and in FAK-null fibroblasts, adhesion-induced FAK activity increased Rab5-GTP levels. In fact, expression of WT FAK and FAK/Y180A/M183A (open conformation), but not FAK/Arg

Identifiants

pubmed: 31292193
pii: S0021-9258(20)30315-X
doi: 10.1074/jbc.RA119.008667
pmc: PMC6709621
doi:

Substances chimiques

Focal Adhesion Kinase 1 EC 2.7.10.2
PTK2 protein, human EC 2.7.10.2
RAB5C protein, human EC 3.6.1.-
rab5 GTP-Binding Proteins EC 3.6.5.2

Types de publication

Journal Article Research Support, Non-U.S. Gov't

Langues

eng

Sous-ensembles de citation

IM

Pagination

12836-12845

Informations de copyright

© 2019 Arriagada et al.

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Auteurs

Cecilia Arriagada (C)

Institute for Research in Dental Sciences, Faculty of Dentistry, Universidad de Chile, Santiago 8380000, Chile.

Patricio Silva (P)

Institute for Research in Dental Sciences, Faculty of Dentistry, Universidad de Chile, Santiago 8380000, Chile.
Faculty of Health Sciences, Universidad Central de Chile, Santiago 8380000, Chile.

Martial Millet (M)

Institute for Research in Dental Sciences, Faculty of Dentistry, Universidad de Chile, Santiago 8380000, Chile.

Luis Solano (L)

Institute for Research in Dental Sciences, Faculty of Dentistry, Universidad de Chile, Santiago 8380000, Chile.

Carolina Moraga (C)

Institute for Research in Dental Sciences, Faculty of Dentistry, Universidad de Chile, Santiago 8380000, Chile.

Vicente A Torres (VA)

Institute for Research in Dental Sciences, Faculty of Dentistry, Universidad de Chile, Santiago 8380000, Chile vatorres@med.uchile.cl.
Advanced Center for Chronic Diseases, Universidad de Chile, Santiago 8380000, Chile.

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Classifications MeSH