Phosphatidylinositol 4-kinasebeta is critical for functional association of rab11 with the Golgi complex

Petra de Graaf; Wilbert T Zwart; Remco A J van Dijken; Magdalena Deneka; Thomas K F Schulz; Niels Geijsen; Paul J Coffer; Bart M Gadella; Arie J Verkleij; Peter van der Sluijs; Paul M P van Bergen en Henegouwen

doi:10.1091/mbc.e03-12-0862

Phosphatidylinositol 4-kinasebeta is critical for functional association of rab11 with the Golgi complex

Petra de Graaf, Wilbert T Zwart, Remco A J van Dijken, Magdalena Deneka, Thomas K F Schulz, Niels Geijsen, Paul J Coffer, Bart M Gadella, Arie J Verkleij, Peter van der Sluijs, Paul M P van Bergen en Henegouwen

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

Abstract

Phosphatidylinositol 4-kinasebeta (PI4Kbeta) plays an essential role in maintaining the structural integrity of the Golgi complex. In a search for PI4Kbeta-interacting proteins, we found that PI4Kbeta specifically interacts with the GTP-bound form of the small GTPase rab11. The PI4Kbeta-rab11 interaction is of functional significance because inhibition of rab11 binding to PI4Kbeta abolished the localization of rab11 to the Golgi complex and significantly inhibited transport of vesicular stomatitis virus G protein from the Golgi complex to the plasma membrane. We propose that a novel function of PI4Kbeta is to act as a docking protein for rab11 in the Golgi complex, which is important for biosynthetic membrane transport from the Golgi complex to the plasma membrane.

Original language	English
Pages (from-to)	2038-47
Number of pages	10
Journal	Molecular Biology of the Cell
Volume	15
Issue number	4
DOIs	https://doi.org/10.1091/mbc.e03-12-0862
Publication status	Published - Apr 2004

Keywords

Animals
Binding Sites
Biological Transport
Brefeldin A
COS Cells
Cell Membrane
Cricetinae
DNA
DNA, Complementary
Glutathione Transferase
Golgi Apparatus
Green Fluorescent Proteins
Guanosine Triphosphate
Luminescent Proteins
Membrane Glycoproteins
Microscopy, Fluorescence
Phosphotransferases (Alcohol Group Acceptor)
Protein Binding
Protein Structure, Tertiary
Saccharomyces cerevisiae
Transfection
Two-Hybrid System Techniques
Viral Envelope Proteins
beta-Galactosidase
rab GTP-Binding Proteins
Journal Article
Research Support, Non-U.S. Gov't

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10.1091/mbc.e03-12-0862

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de Graaf, P., Zwart, W. T., van Dijken, R. A. J., Deneka, M., Schulz, T. K. F., Geijsen, N., Coffer, P. J., Gadella, B. M., Verkleij, A. J., van der Sluijs, P., & van Bergen en Henegouwen, P. M. P. (2004). Phosphatidylinositol 4-kinasebeta is critical for functional association of rab11 with the Golgi complex. Molecular Biology of the Cell, 15(4), 2038-47. https://doi.org/10.1091/mbc.e03-12-0862

@article{1c22ea1a122f42debe554d6073826723,

title = "Phosphatidylinositol 4-kinasebeta is critical for functional association of rab11 with the Golgi complex",

abstract = "Phosphatidylinositol 4-kinasebeta (PI4Kbeta) plays an essential role in maintaining the structural integrity of the Golgi complex. In a search for PI4Kbeta-interacting proteins, we found that PI4Kbeta specifically interacts with the GTP-bound form of the small GTPase rab11. The PI4Kbeta-rab11 interaction is of functional significance because inhibition of rab11 binding to PI4Kbeta abolished the localization of rab11 to the Golgi complex and significantly inhibited transport of vesicular stomatitis virus G protein from the Golgi complex to the plasma membrane. We propose that a novel function of PI4Kbeta is to act as a docking protein for rab11 in the Golgi complex, which is important for biosynthetic membrane transport from the Golgi complex to the plasma membrane.",

keywords = "Animals, Binding Sites, Biological Transport, Brefeldin A, COS Cells, Cell Membrane, Cricetinae, DNA, DNA, Complementary, Glutathione Transferase, Golgi Apparatus, Green Fluorescent Proteins, Guanosine Triphosphate, Luminescent Proteins, Membrane Glycoproteins, Microscopy, Fluorescence, Phosphotransferases (Alcohol Group Acceptor), Protein Binding, Protein Structure, Tertiary, Saccharomyces cerevisiae, Transfection, Two-Hybrid System Techniques, Viral Envelope Proteins, beta-Galactosidase, rab GTP-Binding Proteins, Journal Article, Research Support, Non-U.S. Gov't",

author = "{de Graaf}, Petra and Zwart, {Wilbert T} and {van Dijken}, {Remco A J} and Magdalena Deneka and Schulz, {Thomas K F} and Niels Geijsen and Coffer, {Paul J} and Gadella, {Bart M} and Verkleij, {Arie J} and {van der Sluijs}, Peter and {van Bergen en Henegouwen}, {Paul M P}",

year = "2004",

month = apr,

doi = "10.1091/mbc.e03-12-0862",

language = "English",

volume = "15",

pages = "2038--47",

journal = "Molecular Biology of the Cell",

issn = "1059-1524",

publisher = "American Society for Cell Biology",

number = "4",

}

de Graaf, P, Zwart, WT, van Dijken, RAJ, Deneka, M, Schulz, TKF, Geijsen, N, Coffer, PJ, Gadella, BM, Verkleij, AJ, van der Sluijs, P & van Bergen en Henegouwen, PMP 2004, 'Phosphatidylinositol 4-kinasebeta is critical for functional association of rab11 with the Golgi complex', Molecular Biology of the Cell, vol. 15, no. 4, pp. 2038-47. https://doi.org/10.1091/mbc.e03-12-0862

TY - JOUR

T1 - Phosphatidylinositol 4-kinasebeta is critical for functional association of rab11 with the Golgi complex

AU - de Graaf, Petra

AU - Zwart, Wilbert T

AU - van Dijken, Remco A J

AU - Deneka, Magdalena

AU - Schulz, Thomas K F

AU - Geijsen, Niels

AU - Coffer, Paul J

AU - Gadella, Bart M

AU - Verkleij, Arie J

AU - van der Sluijs, Peter

AU - van Bergen en Henegouwen, Paul M P

PY - 2004/4

Y1 - 2004/4

N2 - Phosphatidylinositol 4-kinasebeta (PI4Kbeta) plays an essential role in maintaining the structural integrity of the Golgi complex. In a search for PI4Kbeta-interacting proteins, we found that PI4Kbeta specifically interacts with the GTP-bound form of the small GTPase rab11. The PI4Kbeta-rab11 interaction is of functional significance because inhibition of rab11 binding to PI4Kbeta abolished the localization of rab11 to the Golgi complex and significantly inhibited transport of vesicular stomatitis virus G protein from the Golgi complex to the plasma membrane. We propose that a novel function of PI4Kbeta is to act as a docking protein for rab11 in the Golgi complex, which is important for biosynthetic membrane transport from the Golgi complex to the plasma membrane.

AB - Phosphatidylinositol 4-kinasebeta (PI4Kbeta) plays an essential role in maintaining the structural integrity of the Golgi complex. In a search for PI4Kbeta-interacting proteins, we found that PI4Kbeta specifically interacts with the GTP-bound form of the small GTPase rab11. The PI4Kbeta-rab11 interaction is of functional significance because inhibition of rab11 binding to PI4Kbeta abolished the localization of rab11 to the Golgi complex and significantly inhibited transport of vesicular stomatitis virus G protein from the Golgi complex to the plasma membrane. We propose that a novel function of PI4Kbeta is to act as a docking protein for rab11 in the Golgi complex, which is important for biosynthetic membrane transport from the Golgi complex to the plasma membrane.

KW - Animals

KW - Binding Sites

KW - Biological Transport

KW - Brefeldin A

KW - COS Cells

KW - Cell Membrane

KW - Cricetinae

KW - DNA

KW - DNA, Complementary

KW - Glutathione Transferase

KW - Golgi Apparatus

KW - Green Fluorescent Proteins

KW - Guanosine Triphosphate

KW - Luminescent Proteins

KW - Membrane Glycoproteins

KW - Microscopy, Fluorescence

KW - Phosphotransferases (Alcohol Group Acceptor)

KW - Protein Binding

KW - Protein Structure, Tertiary

KW - Saccharomyces cerevisiae

KW - Transfection

KW - Two-Hybrid System Techniques

KW - Viral Envelope Proteins

KW - beta-Galactosidase

KW - rab GTP-Binding Proteins

KW - Journal Article

KW - Research Support, Non-U.S. Gov't

U2 - 10.1091/mbc.e03-12-0862

DO - 10.1091/mbc.e03-12-0862

M3 - Article

C2 - 14767056

SN - 1059-1524

VL - 15

SP - 2038

EP - 2047

JO - Molecular Biology of the Cell

JF - Molecular Biology of the Cell

IS - 4

ER -

Phosphatidylinositol 4-kinasebeta is critical for functional association of rab11 with the Golgi complex

Abstract

Keywords

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