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

IUBMB Life. 2002 Jan;53(1):15-23. doi: 10.1080/15216540210814.

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.

Publication types

  • Review

MeSH terms

  • Amino Acid Sequence
  • Animals
  • Carbon-Oxygen Lyases / chemistry
  • Carbon-Oxygen Lyases / 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
  • Nerve Tissue Proteins / genetics
  • Nerve Tissue Proteins / metabolism
  • Phosphoric Monoester Hydrolases / chemistry*
  • Phosphoric Monoester Hydrolases / genetics
  • Phosphoric Monoester Hydrolases / metabolism*
  • Protein Structure, Tertiary
  • Signal Transduction
  • Substrate Specificity

Substances

  • Nerve Tissue Proteins
  • synaptojanin
  • Phosphoric Monoester Hydrolases
  • Inositol Polyphosphate 5-Phosphatases
  • Carbon-Oxygen Lyases
  • DNA-(Apurinic or Apyrimidinic Site) Lyase