PSTPIP1 and PSTPIP2/MAYP

Violeta Chitu; E. Richard Stanley

doi:10.1201/9781498712798-11

PSTPIP1 and PSTPIP2/MAYP

Violeta Chitu, E. Richard Stanley

Developmental & Molecular Biology

Research output: Chapter in Book/Report/Conference proceeding › Chapter

3 Scopus citations

Abstract

PSTPIP1 and PSTPIP2 are expressed predominantly in the hematopoietic system where their C-terminal tyrosine phosphorylation is regulated by PEST family phosphatases. Both proteins deform membranes via their conserved F-BAR domains and regulate actin organization, but their actin regulatory activities differ. PSTPIPl negatively regulates actin po lymerization by recruiting PTP-PEST to WASP and mediating dephosphorylation o f WASP at Y291. PSTPIP2 bundles actin and increases filopodia formation. Mutations in human PSTPIPl and mouse PSTPIP2 cause autoinflammatory diseases. Analysis o f the actions o f these proteins promises to reveal novel mechanisms for the regulation o f the inflammatory response involving macrophages and osteoclasts.

Original language	English (US)
Title of host publication	The Pombe Cdc15 Homology Proteins
Publisher	CRC Press
Pages	49-61
Number of pages	13
ISBN (Electronic)	9781498712798
ISBN (Print)	9781587063138
DOIs	https://doi.org/10.1201/9781498712798-11
State	Published - Jan 1 2009

ASJC Scopus subject areas

General Agricultural and Biological Sciences
General Biochemistry, Genetics and Molecular Biology

UN SDGs

This output contributes to the following UN Sustainable Development Goals (SDGs)

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10.1201/9781498712798-11

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abstract = "PSTPIP1 and PSTPIP2 are expressed predominantly in the hematopoietic system where their C-terminal tyrosine phosphorylation is regulated by PEST family phosphatases. Both proteins deform membranes via their conserved F-BAR domains and regulate actin organization, but their actin regulatory activities differ. PSTPIPl negatively regulates actin po lymerization by recruiting PTP-PEST to WASP and mediating dephosphorylation o f WASP at Y291. PSTPIP2 bundles actin and increases filopodia formation. Mutations in human PSTPIPl and mouse PSTPIP2 cause autoinflammatory diseases. Analysis o f the actions o f these proteins promises to reveal novel mechanisms for the regulation o f the inflammatory response involving macrophages and osteoclasts.",

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AB - PSTPIP1 and PSTPIP2 are expressed predominantly in the hematopoietic system where their C-terminal tyrosine phosphorylation is regulated by PEST family phosphatases. Both proteins deform membranes via their conserved F-BAR domains and regulate actin organization, but their actin regulatory activities differ. PSTPIPl negatively regulates actin po lymerization by recruiting PTP-PEST to WASP and mediating dephosphorylation o f WASP at Y291. PSTPIP2 bundles actin and increases filopodia formation. Mutations in human PSTPIPl and mouse PSTPIP2 cause autoinflammatory diseases. Analysis o f the actions o f these proteins promises to reveal novel mechanisms for the regulation o f the inflammatory response involving macrophages and osteoclasts.

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ER -

PSTPIP1 and PSTPIP2/MAYP

Abstract

ASJC Scopus subject areas

UN SDGs

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