A conserved family of enzymes that phosphorylate inositol hexakisphosphate.

Published

Journal Article

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 (IP6) and inositol heptakisphosphate (IP7) 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 IP6.

Full Text

Duke Authors

Cited Authors

  • Mulugu, S; Bai, W; Fridy, PC; Bastidas, RJ; Otto, JC; Dollins, DE; Haystead, TA; Ribeiro, AA; York, JD

Published Date

  • April 6, 2007

Published In

Volume / Issue

  • 316 / 5821

Start / End Page

  • 106 - 109

PubMed ID

  • 17412958

Pubmed Central ID

  • 17412958

Electronic International Standard Serial Number (EISSN)

  • 1095-9203

Digital Object Identifier (DOI)

  • 10.1126/science.1139099

Language

  • eng

Conference Location

  • United States