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Rac1-PAK1 regulation of Rab11 cycling promotes junction destabilization
Author(s) -
Jennifer C. Erasmus,
Kasia Smolarczyk,
Helena Brezovjakova,
Noor Faizah MohdNaim,
Encarnación Lozano,
Karl Matter,
Vania Braga
Publication year - 2021
Publication title -
the journal of cell biology
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 5.414
H-Index - 380
eISSN - 1540-8140
pISSN - 0021-9525
DOI - 10.1083/jcb.202002114
Subject(s) - rab , pak1 , microbiology and biotechnology , rac1 , biology , gtpase , internalization , exocytosis , phosphorylation , cadherin , membrane , biochemistry , signal transduction , cell
Rac1 promotes malignancy. Oncogenic Rac1 and its effector PAK1 disrupt junctions via internalization of cadherin adhesion receptors by bulk fluid uptake. PAK1 phosphorylates a key regulator of intracellular trafficking, RabGDIβ, thereby modulating its affinity with specific partners (i.e., Rab11) to re-route cadherin away from cell–cell contacts.

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