ArticleOncogene1999
Mechanism of activation of Pak1 kinase by membrane localization.
Article in Oncogene, 1999. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 33 papers.
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Who cites it
33 citing papers in PubMed, 81 citations in OpenAlex.
- Modulating PAK1: Accessory Proteins as Promising Therapeutic Targets.Biomolecules · 2025Review
- Group I PAKs in myelin formation and repair of the central nervous system: what, when, and how.Biological reviews of the Cambridge Philosophical Society · 2022Review
- The Role of p21-Activated Kinases in Cancer and Beyond: Where Are We Heading?Frontiers in cell and developmental biology · 2021Review
- The subcellular localization of type I p21-activated kinases is controlled by the disordered variable region and polybasic sequences.The Journal of biological chemistry · 2019Article
- p27eLife · 2017Article
- Kaposi's sarcoma-associated herpesvirus microRNAs repress breakpoint cluster region protein expression, enhance Rac1 activity, and increase in vitro angiogenesis.Journal of virology · 2015Article
- Republished: tracing PAKs from GI inflammation to cancer.Postgraduate medical journal · 2014Article
- Maturin is a novel protein required for differentiation during primary neurogenesis.Developmental biology · 2013Article
- Structurally unique interaction of RBD-like and PH domains is crucial for yeast pheromone signaling.Molecular biology of the cell · 2013Article
- Altered nitric oxide production mediates matrix-specific PAK2 and NF-κB activation by flow.Molecular biology of the cell · 2013Article
- Functions and regulation of circular dorsal ruffles.Molecular and cellular biology · 2012Review
- Regulation of adherens junction dynamics by phosphorylation switches.Journal of signal transduction · 2012Article
- SH3BP1, an exocyst-associated RhoGAP, inactivates Rac1 at the front to drive cell motility.Molecular cell · 2011Article
- Inhibition of Cdc42-mediated activation of mixed lineage kinase 3 by the tumor suppressor protein merlin.Small GTPases · 2010Article
- Dissecting activation of the PAK1 kinase at protrusions in living cells.The Journal of biological chemistry · 2009Article
- Roles of P21-activated kinases and associated proteins in epithelial wound healing.International review of cell and molecular biology · 2008Review
- BCR and its mutants, the reciprocal t(9;22)-associated ABL/BCR fusion proteins, differentially regulate the cytoskeleton and cell motility.BMC cancer · 2006Article
- Requirement of Nck adaptors for actin dynamics and cell migration stimulated by platelet-derived growth factor B.Proceedings of the National Academy of Sciences of the United States of America · 2006Article
- Bcr is a negative regulator of the Wnt signalling pathway.EMBO reports · 2005Article
- Binding of activated alpha2-macroglobulin to its cell surface receptor GRP78 in 1-LN prostate cancer cells regulates PAK-2-dependent activation of LIMK.The Journal of biological chemistry · 2005Article
Corrections and comments
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Authors and funding
2 authors at 1 institution in 1 country.
Funding
No grant is acknowledged in the PubMed record.
Abstract
Pak kinases are a family of serine/threonine protein kinases homologous to Ste20p of yeast. Paks can be activated in vivo and in vitro by binding to GTP-bound Cdc42 and Rac1, members of the Rho family of small GTPases implicated in regulating the organization of the actin cytoskeleton. We have previously reported that the SH2/SH3-containing adaptor protein Nck binds Pak kinase through its second SH3 domain. Pak1 can be targeted to the membrane by Nck in response to tyrosine phosphorylation, and membrane association of Pak1 is sufficient to increase its specific activity. The mechanism whereby Pak is activated by membrane localization, however, is unknown. We show here that expression of three proteins that inhibit Rho-family GTPases by different mechanisms (RhoGDI, Bcr and D57Y Cdc42) all block the activation of Pak by a membrane-targeted Nck SH3 domain, demonstrating that the in vivo activation of Pak1 induced by membrane localization is dependent on Rho-family GTPases. This implies that Pak activity can be regulated in cells both by the level of GTP loading of various Rho-family GTPases and the local concentration of Pak relative to these GTPases. Our data also suggest the existence of Rho-family GTPases in addition to Cdc42 and Rac1 that can activate Pak on membranes.
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Registered trials
Read under generation 80e0d062 · epoch 390. Bibliography from PubMed, PubMed Central and OpenAlex; grants from NIH RePORTER; trial links from ClinicalTrials.gov; estimates, votes and beliefs from the OpenQuestion graph.