Phosphatidylinositol 4 phosphate regulates targeting of clathrin adaptor AP-1 complexes to the Golgi

Ying Jie Wang, Jing Wang, Hui Qiao Sun, Manuel Martinez, Yu Xiao Sun, Eric Macia, Tomas Kirchhausen, Joseph P. Albanesi, Michael G. Roth, Helen L. Yin

Research output: Contribution to journalArticle

381 Citations (Scopus)

Abstract

Phosphatidylinositol 4 phosphate [PI(4)P] is essential for secretion in yeast, but its role in mammalian cells is unclear. Current paradigms propose that PI(4)P acts primarily as a precursor to phosphatidylinositol 4,5 bisphosphate (PIP2), an important plasma membrane regulator. We found that PI(4)P is enriched in the mammalian Golgi, and used RNA interference (RNAi) of PI4KIIα, a Golgi resident phosphatidylinositol 4 kinase, to determine whether PI(4)P directly regulates the Golgi. PI4KIIα RNAi decreases Golgi PI(4)P, blocks the recruitment of clathrin adaptor AP-1 complexes to the Golgi, and inhibits AP-1-dependent functions. This AP-1 binding defect is rescued by adding back PI(4)P. In addition, purified AP-1 binds PI(4)P, and anti-PI(4)P inhibits the in vitro recruitment of cytosolic AP-1 to normal cellular membranes. We propose that PI4KIIα establishes the Golgi's unique lipid-defined organelle identity by generating PI(4)P-rich domains that specify the docking of the AP-1 coat machinery.

Original languageEnglish (US)
Pages (from-to)299-310
Number of pages12
JournalCell
Volume114
Issue number3
DOIs
StatePublished - Aug 8 2003

Fingerprint

Vesicular Transport Adaptor Proteins
Transcription Factor AP-1
Golgi Apparatus
RNA Interference
RNA
1-Phosphatidylinositol 4-Kinase
phosphatidylinositol 4-phosphate
Cell membranes
Phosphatidylinositols
Organelles
Yeast
Machinery
Yeasts
Cells
Cell Membrane
Membranes
Lipids
Defects

ASJC Scopus subject areas

  • Cell Biology
  • Molecular Biology

Cite this

Phosphatidylinositol 4 phosphate regulates targeting of clathrin adaptor AP-1 complexes to the Golgi. / Wang, Ying Jie; Wang, Jing; Sun, Hui Qiao; Martinez, Manuel; Sun, Yu Xiao; Macia, Eric; Kirchhausen, Tomas; Albanesi, Joseph P.; Roth, Michael G.; Yin, Helen L.

In: Cell, Vol. 114, No. 3, 08.08.2003, p. 299-310.

Research output: Contribution to journalArticle

Wang, Ying Jie ; Wang, Jing ; Sun, Hui Qiao ; Martinez, Manuel ; Sun, Yu Xiao ; Macia, Eric ; Kirchhausen, Tomas ; Albanesi, Joseph P. ; Roth, Michael G. ; Yin, Helen L. / Phosphatidylinositol 4 phosphate regulates targeting of clathrin adaptor AP-1 complexes to the Golgi. In: Cell. 2003 ; Vol. 114, No. 3. pp. 299-310.
@article{8467dc869b15496fa04a9ae5826f7157,
title = "Phosphatidylinositol 4 phosphate regulates targeting of clathrin adaptor AP-1 complexes to the Golgi",
abstract = "Phosphatidylinositol 4 phosphate [PI(4)P] is essential for secretion in yeast, but its role in mammalian cells is unclear. Current paradigms propose that PI(4)P acts primarily as a precursor to phosphatidylinositol 4,5 bisphosphate (PIP2), an important plasma membrane regulator. We found that PI(4)P is enriched in the mammalian Golgi, and used RNA interference (RNAi) of PI4KIIα, a Golgi resident phosphatidylinositol 4 kinase, to determine whether PI(4)P directly regulates the Golgi. PI4KIIα RNAi decreases Golgi PI(4)P, blocks the recruitment of clathrin adaptor AP-1 complexes to the Golgi, and inhibits AP-1-dependent functions. This AP-1 binding defect is rescued by adding back PI(4)P. In addition, purified AP-1 binds PI(4)P, and anti-PI(4)P inhibits the in vitro recruitment of cytosolic AP-1 to normal cellular membranes. We propose that PI4KIIα establishes the Golgi's unique lipid-defined organelle identity by generating PI(4)P-rich domains that specify the docking of the AP-1 coat machinery.",
author = "Wang, {Ying Jie} and Jing Wang and Sun, {Hui Qiao} and Manuel Martinez and Sun, {Yu Xiao} and Eric Macia and Tomas Kirchhausen and Albanesi, {Joseph P.} and Roth, {Michael G.} and Yin, {Helen L.}",
year = "2003",
month = "8",
day = "8",
doi = "10.1016/S0092-8674(03)00603-2",
language = "English (US)",
volume = "114",
pages = "299--310",
journal = "Cell",
issn = "0092-8674",
publisher = "Cell Press",
number = "3",

}

TY - JOUR

T1 - Phosphatidylinositol 4 phosphate regulates targeting of clathrin adaptor AP-1 complexes to the Golgi

AU - Wang, Ying Jie

AU - Wang, Jing

AU - Sun, Hui Qiao

AU - Martinez, Manuel

AU - Sun, Yu Xiao

AU - Macia, Eric

AU - Kirchhausen, Tomas

AU - Albanesi, Joseph P.

AU - Roth, Michael G.

AU - Yin, Helen L.

PY - 2003/8/8

Y1 - 2003/8/8

N2 - Phosphatidylinositol 4 phosphate [PI(4)P] is essential for secretion in yeast, but its role in mammalian cells is unclear. Current paradigms propose that PI(4)P acts primarily as a precursor to phosphatidylinositol 4,5 bisphosphate (PIP2), an important plasma membrane regulator. We found that PI(4)P is enriched in the mammalian Golgi, and used RNA interference (RNAi) of PI4KIIα, a Golgi resident phosphatidylinositol 4 kinase, to determine whether PI(4)P directly regulates the Golgi. PI4KIIα RNAi decreases Golgi PI(4)P, blocks the recruitment of clathrin adaptor AP-1 complexes to the Golgi, and inhibits AP-1-dependent functions. This AP-1 binding defect is rescued by adding back PI(4)P. In addition, purified AP-1 binds PI(4)P, and anti-PI(4)P inhibits the in vitro recruitment of cytosolic AP-1 to normal cellular membranes. We propose that PI4KIIα establishes the Golgi's unique lipid-defined organelle identity by generating PI(4)P-rich domains that specify the docking of the AP-1 coat machinery.

AB - Phosphatidylinositol 4 phosphate [PI(4)P] is essential for secretion in yeast, but its role in mammalian cells is unclear. Current paradigms propose that PI(4)P acts primarily as a precursor to phosphatidylinositol 4,5 bisphosphate (PIP2), an important plasma membrane regulator. We found that PI(4)P is enriched in the mammalian Golgi, and used RNA interference (RNAi) of PI4KIIα, a Golgi resident phosphatidylinositol 4 kinase, to determine whether PI(4)P directly regulates the Golgi. PI4KIIα RNAi decreases Golgi PI(4)P, blocks the recruitment of clathrin adaptor AP-1 complexes to the Golgi, and inhibits AP-1-dependent functions. This AP-1 binding defect is rescued by adding back PI(4)P. In addition, purified AP-1 binds PI(4)P, and anti-PI(4)P inhibits the in vitro recruitment of cytosolic AP-1 to normal cellular membranes. We propose that PI4KIIα establishes the Golgi's unique lipid-defined organelle identity by generating PI(4)P-rich domains that specify the docking of the AP-1 coat machinery.

UR - http://www.scopus.com/inward/record.url?scp=0042591490&partnerID=8YFLogxK

UR - http://www.scopus.com/inward/citedby.url?scp=0042591490&partnerID=8YFLogxK

U2 - 10.1016/S0092-8674(03)00603-2

DO - 10.1016/S0092-8674(03)00603-2

M3 - Article

C2 - 12914695

AN - SCOPUS:0042591490

VL - 114

SP - 299

EP - 310

JO - Cell

JF - Cell

SN - 0092-8674

IS - 3

ER -