Structure-function relationships of phosphatidylinositol transfer proteins: involvement of phosphorylation sites

Gerry T. Snoek; Claudia M. van Tiel; Maarten R. Egmond

doi:https://doi.org/10.1016/j.biochi.2004.09.021

Structure-function relationships of phosphatidylinositol transfer proteins: involvement of phosphorylation sites

Gerry T. Snoek, Claudia M. van Tiel, Maarten R. Egmond

Research output: Contribution to journal › Article › Academic › peer-review

4 Citations (Scopus)

Abstract

The mammalian low molecular weight phosphatidylinositol transfer proteins: PI-TPalpha and PI-TPbeta are extremely well conserved and highly homologous. Surprisingly, the two proteins clearly show different cellular localizations and display contrary physiological functions. Phosphorylation of the proteins might be the regulatory factor to ensure the selective cellular functions. A major difference between PI-TPalpha and PI-TPbeta is the capacity of PI-TPbeta to bind and transfer sphingomyelin (SM) in vivo. This activity is correlated with phosphorylation of Ser262, which is only present in PI-TPbeta. Structural aspects of phosphorylation sites of PI-TPs are analyzed in order to find an explanation for the functional data. We propose that phosphorylation of one serine residue (Ser165/166) in both PI-TPalpha and PI-TPbeta is involved in the regulation of membrane binding of all PI-TPs and that phosphorylation of the unique Ser262 in PI-TPbeta-like proteins ensures the right cellular localization of PI-TPbetas that is necessary for the specific activity at the Golgi membrane

Original language	English
Pages (from-to)	857-864
Journal	Biochimie
Volume	86
Issue number	11
DOIs	https://doi.org/10.1016/j.biochi.2004.09.021
Publication status	Published - 2004

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https://doi.org/10.1016/j.biochi.2004.09.021

Cite this

@article{ea4e4e2cbdaf470c954c781d060f297b,

title = "Structure-function relationships of phosphatidylinositol transfer proteins: involvement of phosphorylation sites",

abstract = "The mammalian low molecular weight phosphatidylinositol transfer proteins: PI-TPalpha and PI-TPbeta are extremely well conserved and highly homologous. Surprisingly, the two proteins clearly show different cellular localizations and display contrary physiological functions. Phosphorylation of the proteins might be the regulatory factor to ensure the selective cellular functions. A major difference between PI-TPalpha and PI-TPbeta is the capacity of PI-TPbeta to bind and transfer sphingomyelin (SM) in vivo. This activity is correlated with phosphorylation of Ser262, which is only present in PI-TPbeta. Structural aspects of phosphorylation sites of PI-TPs are analyzed in order to find an explanation for the functional data. We propose that phosphorylation of one serine residue (Ser165/166) in both PI-TPalpha and PI-TPbeta is involved in the regulation of membrane binding of all PI-TPs and that phosphorylation of the unique Ser262 in PI-TPbeta-like proteins ensures the right cellular localization of PI-TPbetas that is necessary for the specific activity at the Golgi membrane",

author = "Snoek, {Gerry T.} and {van Tiel}, {Claudia M.} and Egmond, {Maarten R.}",

year = "2004",

doi = "https://doi.org/10.1016/j.biochi.2004.09.021",

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TY - JOUR

T1 - Structure-function relationships of phosphatidylinositol transfer proteins: involvement of phosphorylation sites

AU - Snoek, Gerry T.

AU - van Tiel, Claudia M.

AU - Egmond, Maarten R.

PY - 2004

Y1 - 2004

N2 - The mammalian low molecular weight phosphatidylinositol transfer proteins: PI-TPalpha and PI-TPbeta are extremely well conserved and highly homologous. Surprisingly, the two proteins clearly show different cellular localizations and display contrary physiological functions. Phosphorylation of the proteins might be the regulatory factor to ensure the selective cellular functions. A major difference between PI-TPalpha and PI-TPbeta is the capacity of PI-TPbeta to bind and transfer sphingomyelin (SM) in vivo. This activity is correlated with phosphorylation of Ser262, which is only present in PI-TPbeta. Structural aspects of phosphorylation sites of PI-TPs are analyzed in order to find an explanation for the functional data. We propose that phosphorylation of one serine residue (Ser165/166) in both PI-TPalpha and PI-TPbeta is involved in the regulation of membrane binding of all PI-TPs and that phosphorylation of the unique Ser262 in PI-TPbeta-like proteins ensures the right cellular localization of PI-TPbetas that is necessary for the specific activity at the Golgi membrane

AB - The mammalian low molecular weight phosphatidylinositol transfer proteins: PI-TPalpha and PI-TPbeta are extremely well conserved and highly homologous. Surprisingly, the two proteins clearly show different cellular localizations and display contrary physiological functions. Phosphorylation of the proteins might be the regulatory factor to ensure the selective cellular functions. A major difference between PI-TPalpha and PI-TPbeta is the capacity of PI-TPbeta to bind and transfer sphingomyelin (SM) in vivo. This activity is correlated with phosphorylation of Ser262, which is only present in PI-TPbeta. Structural aspects of phosphorylation sites of PI-TPs are analyzed in order to find an explanation for the functional data. We propose that phosphorylation of one serine residue (Ser165/166) in both PI-TPalpha and PI-TPbeta is involved in the regulation of membrane binding of all PI-TPs and that phosphorylation of the unique Ser262 in PI-TPbeta-like proteins ensures the right cellular localization of PI-TPbetas that is necessary for the specific activity at the Golgi membrane

U2 - https://doi.org/10.1016/j.biochi.2004.09.021

DO - https://doi.org/10.1016/j.biochi.2004.09.021

M3 - Article

C2 - 15589696

SN - 0300-9084

VL - 86

SP - 857

EP - 864

JO - Biochimie

JF - Biochimie

IS - 11

ER -