Ontology highlight
ABSTRACT:
SUBMITTER: Bhandari R
PROVIDER: S-EPMC2000531 | biostudies-literature | 2007 Sep
REPOSITORIES: biostudies-literature
Bhandari Rashna R Saiardi Adolfo A Ahmadibeni Yousef Y Snowman Adele M AM Resnick Adam C AC Kristiansen Troels Z TZ Molina Henrik H Pandey Akhilesh A Werner J Kent JK Juluri Krishna R KR Xu Yong Y Prestwich Glenn D GD Parang Keykavous K Snyder Solomon H SH
Proceedings of the National Academy of Sciences of the United States of America 20070914 39
In a previous study, we showed that the inositol pyrophosphate diphosphoinositol pentakisphosphate (IP(7)) physiologically phosphorylates mammalian and yeast proteins. We now report that this phosphate transfer reflects pyrophosphorylation. Thus, proteins must be prephosphorylated by ATP to prime them for IP(7) phosphorylation. IP(7) phosphorylates synthetic phosphopeptides but not if their phosphates have been masked by methylation or pyrophosphorylation. Moreover, IP(7) phosphorylated peptides ...[more]