The Arf-GAP and protein scaffold Cat1/Git1 as a multifaceted regulator of cancer progression. (3rd March 2020)

• Record Type: Journal Article
• Authors: Yoo, Sungsoo M.; Cerione, Richard A.; Antonyak, Marc A.
• Is Part Of: Small GTPases. Volume 11:Number 2(2020)
• Page Start: 77
• Page End: 85
• Publication Date: 2020-03-03
• Subjects: Cat1 -- Git1 -- Arf -- GAP -- Cool -- Pix -- cancer -- migration; Guanosine triphosphatase -- Periodicals; Guanosine triphosphatase; Periodicals; 572.793
• DOI: 10.1080/21541248.2017.1362496
• Languages: English
• ISSNs: 2154-1256

Abstract

ABSTRACT: Cool-associated tyrosine phosphorylated protein 1 (Cat1), also referred to as GPCR-kinase interacting protein 1 (Git1), is a ubiquitously expressed, multi-domain protein that is best known for regulating cell shape and migration. Cat1/Git1 functions as a GTPase activating protein (GAP) that inactivates certain members of the ADP-ribosylation factor (Arf) family of small GTPases. It is also a scaffold that brings together several signaling proteins at specific locations within the cell, ensuring their efficient activation. Here we will discuss what is known regarding the classical role of Cat1/Git1 in the regulation of cell morphology and migration, as well as highlight some more recent findings that suggest this interesting signaling/scaffolding protein may also contribute in unexpected ways to oncogenic transformation.