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The Arf-GAP and protein scaffold Cat1/Git1 as a multifaceted regulator of cancer progression.

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.

SUBMITTER: Yoo SM

PROVIDER: S-EPMC7053942 | biostudies-literature | 2020 Mar

REPOSITORIES: biostudies-literature

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The Arf-GAP and protein scaffold Cat1/Git1 as a multifaceted regulator of cancer progression.

Yoo Sungsoo M SM Cerione Richard A RA Antonyak Marc A MA

Small GTPases 20171231 2

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 ...[more]

PMID: 28981399

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