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Phosphatidylinositol transfer protein

From Wikipedia, the free encyclopedia
Phosphatidylinositol transfer protein, beta isoform
Identifiers
SymbolIP_trans
PfamPF02121
InterProIPR001666
SCOP21fvz / SCOPe / SUPFAM
OPM superfamily138
OPM protein2a1l
CDDcd07815
Available protein structures:
Pfam  structures / ECOD  
PDBRCSB PDB; PDBe; PDBj
PDBsumstructure summary

Phosphatidylinositol transfer protein (PITP) or priming in exocytosis protein 3 (PEP3) is a ubiquitous cytosolic domain involved in transport of phospholipids from their site of synthesis in the endoplasmic reticulum and Golgi to other cell membranes.[1][2]

Biological function

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PITP has been also shown to be an essential component of the polyphosphoinositide synthesis machinery and is hence required for proper signalling by epidermal growth factor and f-Met-Leu-Phe, as well as for exocytosis. The role of PITP in polyphosphoinositide synthesis may also explain its involvement in intracellular vesicular traffic.[1]

Structure and evolution

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Along with the structurally unrelated Sec14p family (found in Pfam PF00650), this family can bind/exchange one molecule of phosphatidylinositol (PI) or phosphatidylcholine (PC) and thus aids their transfer between different membrane compartments. There are three sub-families - all share an N-terminal PITP-like domain, whose sequence is highly conserved. It is described as consisting of three regions. The N-terminal region is thought to bind the lipid and contains two helices and an eight-stranded, mostly antiparallel beta-sheet. An intervening loop region, which is thought to play a role in protein-protein interactions, separates this from the C-terminal region, which exhibits the greatest sequence variation and may be involved in membrane binding. This motif marks PITP as part of the larger SRPBCC (START/RHOalphaC/PITP/Bet v1/CoxG/CalC) domain superfamily.[citation needed]

PITP alpha (UniProt Q00169) has a 16-fold greater affinity for PI than PC. Together with PITP beta (UniProt P48739), it is expressed ubiquitously in all tissues.[3]

Human proteins

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The family of human phosphatidylinositol transfer proteins has several members:

References

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  1. ^ a b Liscovitch M, Cantley LC (1995). "Signal transduction and membrane traffic: the PITP/phosphoinositide connection". Cell. 81 (5): 659–662. doi:10.1016/0092-8674(95)90525-1. PMID 7774006.
  2. ^ Hay JC, Martin TF (December 1993). "Phosphatidylinositol transfer protein required for ATP-dependent priming of Ca(2+)-activated secretion". Nature. 366 (6455): 572–5. Bibcode:1993Natur.366..572H. doi:10.1038/366572a0. PMID 8255295. S2CID 4348488.
  3. ^ Hsuan J, Cockcroft S (2001). "The PITP family of phosphatidylinositol transfer proteins". Genome Biol. 2 (9): REVIEWS3011. doi:10.1186/gb-2001-2-9-reviews3011. PMC 138965. PMID 11574064.
This article incorporates text from the public domain Pfam and InterPro: IPR001666