Arf GAPs and molecular motors. (4th May 2019)

• Record Type: Journal Article
• Authors: Luo, Ruibai; Reed, Christine E.; Sload, Jeffrey A.; Wordeman, Linda; Randazzo, Paul A.; Chen, Pei-Wen
• Is Part Of: Small GTPases. Volume 10:Number 3(2019)
• Page Start: 196
• Page End: 209
• Publication Date: 2019-05-04
• Subjects: ADP-ribosylation factor GTPase-activating protein -- ADP-ribosylation factors -- AGAP1 -- Arf -- Arf GAP -- ASAP1 -- Kif2A -- kinesin-13 -- NM2A -- nonmuscle myosin 2A; Guanosine triphosphatase -- Periodicals; Guanosine triphosphatase; Periodicals; 572.793
• DOI: 10.1080/21541248.2017.1308850
• Languages: English
• ISSNs: 2154-1256

Abstract

ABSTRACT: Arf GTPase-activating proteins (Arf GAPs) were first identified as regulators of the small GTP-binding proteins ADP-ribosylation factors (Arfs). The Arf GAPs are a large family of proteins in metazoans, outnumbering the Arfs that they regulate. The members of the Arf GAP family have complex domain structures and some have been implicated in particular cellular functions, such as cell migration, or with particular pathologies, such as tumor invasion and metastasis. The specific effects of Arfs sometimes depend on the Arf GAP involved in their regulation. These observations have led to speculation that the Arf GAPs themselves may affect cellular activities in capacities beyond the regulation of Arfs. Recently, 2 Arf GAPs, ASAP1 and AGAP1, have been found to bind directly to and influence the activity of myosins and kinesins, motor proteins associated with filamentous actin and microtubules, respectively. The Arf GAP-motor protein interaction is critical for cellular behaviors involving the actin cytoskeleton and microtubules, such as cell migration and other cell movements. Arfs, then, may function with molecular motors through Arf GAPs to regulate microtubule and actin remodeling.