A Conserved Family of Enzymes That Phosphorylate Inositol Hexakisphosphate-Reference-Cited by-同舟云学术

A Conserved Family of Enzymes That Phosphorylate Inositol Hexakisphosphate

Published:2007-04-06 Issue:5821 Volume:316 Page:106-109
ISSN:0036-8075
Container-title:Science
language:en
Short-container-title:Science

Author:

Mulugu Sashidhar¹²³,Bai Wenli¹²³,Fridy Peter C.¹²³,Bastidas Robert J.¹²³,Otto James C.¹²³,Dollins D. Eric¹²³,Haystead Timothy A.¹²³,Ribeiro Anthony A.¹²³,York John D.¹²³

Affiliation:

1. Howard Hughes Medical Institute, Department of Pharmacology and Cancer Biology, Duke University Medical Center, DUMC 3813, Durham, NC 27710, USA.

2. Department of Pharmacology and Cancer Biology, Duke University Medical Center, Durham, NC 27710, USA.

3. Department of Biochemistry, NMR Center, Duke University Medical Center, Durham, NC 27710, USA.

Abstract

Inositol pyrophosphates are a diverse group of high-energy signaling molecules whose cellular roles remain an active area of study. We report a previously uncharacterized class of inositol pyrophosphate synthase and find it is identical to yeast Vip1 and Asp1 proteins, regulators of actin-related protein-2/3 (ARP 2/3) complexes. Vip1 and Asp1 acted as enzymes that encode inositol hexakisphosphate (IP 6 ) and inositol heptakisphosphate (IP 7 ) kinase activities. Alterations in kinase activity led to defects in cell growth, morphology, and interactions with ARP complex members. The functionality of Asp1 and Vip1 may provide cells with increased signaling capacity through metabolism of IP 6 .

Publisher

American Association for the Advancement of Science (AAAS)

Subject

Multidisciplinary

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