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PROSITE documentation PDOC51455 [for PROSITE entry PS51455]

Phosphatidylinositol phosphate kinase (PIPK) domain profile





Description

Phosphoinositides (PIs) are central to signal transduction and membrane trafficking in all eukaryotes. They are derived from phosphatidylinositol (PtdIns) as the result of phosphorylation of hydroxyl groups at positions 3, 4 or 5 of the PtdIns head group. Phosphatidylinositol phosphate kinases (PIPKs) phosphorylate phosphatidylinositol phosphate (PtdInsP) to phosphatidylinositol bisphosphate (PtdInsP2). Three types of PIPKs are present throughout the eukaryotic kingdoms. Type I (PtdIns4P 5-kinase) and type II (PtdIns5P 4-kinase) generate PtdIns(4,5)P2 from PtdIns4P and PtdIns5P, respectively. Type III PIPK (PtdIns3P 5-kinases) are distinct from the type I and II PIPKs and synthesize PtdIns(3,5)P2 [1,2,3].

The basic structure of PIPKs shared by animals, yeast and plant PIPks consists of a highly conserved central kinase domain and a dimerization domain. PIPK domains have high sequence identity, well-defined motifs and conserved residues. They consist of two α+β subdomains (see <PDB:1BO1>]. The larger N-terminal subdomain contains a seven-stranded antiparallel β sheet and four helices. The C-terminal subdomain contains a five-stranded antiparallel β sheet and four helices [4].

The profile we developed covers the entire PIPK domain.

Last update:

June 2009 / First entry.

Technical section

PROSITE method (with tools and information) covered by this documentation:

PIPK, PS51455; Phosphatidylinositol phosphate kinase (PIPK) domain profile  (MATRIX)


References

1AuthorsBakthavatsalam D. Meijer H.J.G. Noegel A.A. Govers F.
TitleNovel phosphatidylinositol phosphate kinases with a G-protein coupled receptor signature are shared by Dictyostelium and Phytophthora.
SourceTrends Microbiol. 14:378-382(2006).
PubMed ID16876997
DOI10.1016/j.tim.2006.07.006

2AuthorsHeck J.N. Mellman D.L. Ling K. Sun Y. Wagoner M.P. Schill N.J. Anderson R.A.
TitleA conspicuous connection: structure defines function for the phosphatidylinositol-phosphate kinase family.
SourceCrit. Rev. Biochem. Mol. Biol. 42:15-39(2007).
PubMed ID17364683
DOI10.1080/10409230601162752

3AuthorsSaavedra L. Balbi V. Dove S.K. Hiwatashi Y. Mikami K. Sommarin M.
TitleCharacterization of phosphatidylinositol phosphate kinases from the moss Physcomitrella patens: PpPIPK1 and PpPIPK2.
SourcePlant Cell Physiol. 50:595-609(2009).
PubMed ID19188261
DOI10.1093/pcp/pcp018

4AuthorsRao V.D. Misra S. Boronenkov I.V. Anderson R.A. Hurley J.H.
TitleStructure of type IIbeta phosphatidylinositol phosphate kinase: a protein kinase fold flattened for interfacial phosphorylation.
SourceCell 94:829-839(1998).
PubMed ID9753329



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