Phosphatidylinositol 4-Phosphate Formation at ER Exit Sites Regulates ER Export

Anna Blumental-Perry; Charles J. Haney; Kelly M M. Weixel; Simon C. Watkins; Ora A. Weisz; Meir Aridor

doi:10.1016/j.devcel.2006.09.001

Phosphatidylinositol 4-Phosphate Formation at ER Exit Sites Regulates ER Export

Anna Blumental-Perry
, Charles J. Haney
, Kelly M M. Weixel
, Simon C. Watkins
, Ora A. Weisz
, Meir Aridor

Biochemistry

University of Pittsburgh

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

101 Scopus citations

Abstract

The mechanisms that regulate endoplasmic reticulum (ER) exit-site (ERES) assembly and COPII-mediated ER export are currently unknown. We analyzed the role of phosphatidylinositols (PtdIns) in regulating ER export. Utilizing pleckstrin homology domains and a PtdIns phosphatase to specifically sequester or reduce phosphorylated PtdIns levels, we found that PtdIns 4-phosphate (PtsIns4P) is required to promote COPII-mediated ER export. Biochemical and morphological in vitro analysis revealed dynamic and localized PtsIns4P formation at ERES. PtdIns4P was utilized to support Sar1-induced proliferation and constriction of ERES membranes. PtdIns4P also assisted in Sar1-induced COPII nucleation at ERES. Therefore, localized dynamic remodeling of PtdIns marks ERES membranes to regulate COPII-mediated ER export.

Original language	English
Pages (from-to)	671-682
Number of pages	12
Journal	Developmental Cell
Volume	11
Issue number	5
DOIs	https://doi.org/10.1016/j.devcel.2006.09.001
State	Published - Nov 2006

Keywords

CELLBIO

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10.1016/j.devcel.2006.09.001

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title = "Phosphatidylinositol 4-Phosphate Formation at ER Exit Sites Regulates ER Export",

abstract = "The mechanisms that regulate endoplasmic reticulum (ER) exit-site (ERES) assembly and COPII-mediated ER export are currently unknown. We analyzed the role of phosphatidylinositols (PtdIns) in regulating ER export. Utilizing pleckstrin homology domains and a PtdIns phosphatase to specifically sequester or reduce phosphorylated PtdIns levels, we found that PtdIns 4-phosphate (PtsIns4P) is required to promote COPII-mediated ER export. Biochemical and morphological in vitro analysis revealed dynamic and localized PtsIns4P formation at ERES. PtdIns4P was utilized to support Sar1-induced proliferation and constriction of ERES membranes. PtdIns4P also assisted in Sar1-induced COPII nucleation at ERES. Therefore, localized dynamic remodeling of PtdIns marks ERES membranes to regulate COPII-mediated ER export.",

keywords = "CELLBIO",

author = "Anna Blumental-Perry and Haney, \{Charles J.\} and Weixel, \{Kelly M M.\} and Watkins, \{Simon C.\} and Weisz, \{Ora A.\} and Meir Aridor",

year = "2006",

month = nov,

doi = "10.1016/j.devcel.2006.09.001",

language = "English",

volume = "11",

pages = "671--682",

journal = "Developmental Cell",

issn = "1534-5807",

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TY - JOUR

T1 - Phosphatidylinositol 4-Phosphate Formation at ER Exit Sites Regulates ER Export

AU - Blumental-Perry, Anna

AU - Haney, Charles J.

AU - Weixel, Kelly M M.

AU - Watkins, Simon C.

AU - Weisz, Ora A.

AU - Aridor, Meir

PY - 2006/11

Y1 - 2006/11

N2 - The mechanisms that regulate endoplasmic reticulum (ER) exit-site (ERES) assembly and COPII-mediated ER export are currently unknown. We analyzed the role of phosphatidylinositols (PtdIns) in regulating ER export. Utilizing pleckstrin homology domains and a PtdIns phosphatase to specifically sequester or reduce phosphorylated PtdIns levels, we found that PtdIns 4-phosphate (PtsIns4P) is required to promote COPII-mediated ER export. Biochemical and morphological in vitro analysis revealed dynamic and localized PtsIns4P formation at ERES. PtdIns4P was utilized to support Sar1-induced proliferation and constriction of ERES membranes. PtdIns4P also assisted in Sar1-induced COPII nucleation at ERES. Therefore, localized dynamic remodeling of PtdIns marks ERES membranes to regulate COPII-mediated ER export.

AB - The mechanisms that regulate endoplasmic reticulum (ER) exit-site (ERES) assembly and COPII-mediated ER export are currently unknown. We analyzed the role of phosphatidylinositols (PtdIns) in regulating ER export. Utilizing pleckstrin homology domains and a PtdIns phosphatase to specifically sequester or reduce phosphorylated PtdIns levels, we found that PtdIns 4-phosphate (PtsIns4P) is required to promote COPII-mediated ER export. Biochemical and morphological in vitro analysis revealed dynamic and localized PtsIns4P formation at ERES. PtdIns4P was utilized to support Sar1-induced proliferation and constriction of ERES membranes. PtdIns4P also assisted in Sar1-induced COPII nucleation at ERES. Therefore, localized dynamic remodeling of PtdIns marks ERES membranes to regulate COPII-mediated ER export.

KW - CELLBIO

UR - https://www.scopus.com/pages/publications/33750447321

U2 - 10.1016/j.devcel.2006.09.001

DO - 10.1016/j.devcel.2006.09.001

M3 - Article

C2 - 17084359

AN - SCOPUS:33750447321

SN - 1534-5807

VL - 11

SP - 671

EP - 682

JO - Developmental Cell

JF - Developmental Cell

IS - 5

ER -

Phosphatidylinositol 4-Phosphate Formation at ER Exit Sites Regulates ER Export

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