» Articles » PMID: 14607270

Vav Proteins, Masters of the World of Cytoskeleton Organization

Overview
Journal Cell Signal
Date 2003 Nov 11
PMID 14607270
Citations 87
Authors
Affiliations
Soon will be listed here.
Abstract

Vav proteins are evolutionarily conserved from nematodes to mammals and play a pivotal role in many aspects of cellular signaling, coupling cell surface receptors to various effectors functions. In mammals, there are three family members; Vav1 is specifically expressed in the hematopoietic system, whereas Vav2 and Vav3 are more ubiquitously expressed. Vav proteins contain multiple domains that enable their function in various fashions. The participation of the Vav proteins in several processes that require cytoskeletal reorganization, such as the formation of the immunological synapse (IS), phagocytosis, platelet aggregation, spreading, and transformation will be discussed in this review. We will also cover how the Vav proteins succeed in controlling these processes by their function as guanine nucleotide exchange factors (GEFs) for the Rho/Rac family of GTPases. The contribution of the Vav proteins in a GEF-independent manner to the organization of the cytoskeleton will also be deliberated. The scope of this review is to highlight the numerous roles of the Vav signal transducer proteins in actin organization.

Citing Articles

CD47 prevents Rac-mediated phagocytosis through Vav1 dephosphorylation.

Miller W, Mishra A, Sheedy C, Bond A, Gardner B, Montell D bioRxiv. 2025; .

PMID: 39990418 PMC: 11844498. DOI: 10.1101/2025.02.11.637707.


Vav family exchange factors: Potential regulator in atherosclerosis.

Zhang Y, Ren Y, Zhou T, Qian Z, Bao Z Biochem Biophys Rep. 2024; 40:101878.

PMID: 39649800 PMC: 11625217. DOI: 10.1016/j.bbrep.2024.101878.


Unraveling the Oncogenic Potential of VAV1 in Human Cancer: Lessons from Mouse Models.

Shalom B, Salaymeh Y, Risling M, Katzav S Cells. 2023; 12(9).

PMID: 37174676 PMC: 10177506. DOI: 10.3390/cells12091276.


VAV3 regulates glioblastoma cell proliferation, migration, invasion and cancer stem‑like cell self‑renewal.

Miao R, Huang D, Zhao K, Li Y, Zhang X, Cheng Y Mol Med Rep. 2023; 27(4).

PMID: 36960857 PMC: 10073803. DOI: 10.3892/mmr.2023.12981.


Cell surface protein aggregation triggers endocytosis to maintain plasma membrane proteostasis.

Paul D, Stern O, Vallis Y, Dhillon J, Buchanan A, McMahon H Nat Commun. 2023; 14(1):947.

PMID: 36854675 PMC: 9974993. DOI: 10.1038/s41467-023-36496-y.