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PMID: 12018403 Published · ppublish English Journal Article Review

The structure and function of catalytic domains within inositol polyphosphate 5-phosphatases.

IUBMB life ·Vol. 53 ·No. 1 ·2002-01-00 ·Pages 15-23

Whisstock JC, Wiradjaja F, Waters JE, Gurung R

Abstract

Phosphoinositide signaling pathways regulate many essential cellular functions including proliferation, differentiation and survival, cytoskeletal organization, and vesicular trafficking. The inositol polyphosphate 5-phosphatases regulate the cellular levels of several bioactive phosphoinositide species. This review describes the structure and function of the 5-phosphatase and Sac1 catalytic domains of these enzymes. The crystal structure of the 5-phosphatase domain has been solved and shares homology with members of the AP endonuclease family. The phosphoinositide polyphosphatase activity of the Sac1 domain, found in some inositol polyphosphate 5-phosphatases, is defined by a motif, CX5 R(T/S), also found in both protein and lipid phosphatases.

MeSH Terms
Amino Acid Sequence Animals Carbon-Oxygen Lyases/chemistry,genetics Catalytic Domain DNA-(Apurinic or Apyrimidinic Site) Lyase Evolution, Molecular Humans Inositol Polyphosphate 5-Phosphatases Models, Molecular Molecular Sequence Data Nerve Tissue Proteins/chemistry,genetics,metabolism Phosphoric Monoester Hydrolases/chemistry,genetics,metabolism Protein Structure, Tertiary Signal Transduction Substrate Specificity
Chemicals
Nerve Tissue Proteins synaptojanin Phosphoric Monoester Hydrolases Inositol Polyphosphate 5-Phosphatases Carbon-Oxygen Lyases DNA-(Apurinic or Apyrimidinic Site) Lyase
Authors & Affiliations
4 authors, click to expand affiliations / ORCID
Whisstock J C
Department of Biochemistry and Molecular Biology, Monash University, Victoria, Australia. James.Whisstock@med.monash.edu.au
Wiradjaja F
Waters J E
Gurung R
Article Info
Journal
IUBMB life
Abbr.
IUBMB Life
ISSN
1521-6543
Published
2002-01-00
Pages
15-23
Language
English
Region
England
NLM ID
100888706
Subset
IM
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