The Golgi-associated Hook3 protein is a member of a novel family of microtubule-binding proteins

Jason H. Walenta, Aaron J. Didier, Xinran Liu, Helmut Krämer

Research output: Contribution to journalArticle

143 Citations (Scopus)

Abstract

Microtubules are central to the spatial organization of diverse membrane- trafficking systems. Here, we report that Hook proteins constitute a novel family of cytosolic coiled coil proteins that bind to organelles and to microtubules. The conserved NH2-terminal domains of Hook proteins mediate attachment to microtubules, whereas the more divergent COOH-terminal domains mediate the binding to organelles. Human Hook3 bound to Golgi membranes in vitro and was enriched in the cis-Golgi in vivo. Unlike other cis-Golgi-associated proteins, however, a large fraction of Hook3 maintained its juxtanuclear localization after Brefeldin A treatment, indicating a Golgi-independent mechanism for Hook3 localization. Because overexpression of Hook3 caused fragmentation of the Golgi complex, we propose that Hook3 participates in defining the architecture and localization of the mammalian Golgi complex.

Original languageEnglish (US)
Pages (from-to)923-934
Number of pages12
JournalJournal of Cell Biology
Volume152
Issue number5
DOIs
StatePublished - Mar 5 2001

Fingerprint

Microtubule Proteins
Microtubules
Carrier Proteins
Golgi Apparatus
Organelles
Brefeldin A
Proteins
Membranes

Keywords

  • Brefeldin A
  • Endosomes
  • Golgi complex
  • Hook protein
  • Membrane trafficking

ASJC Scopus subject areas

  • Cell Biology

Cite this

The Golgi-associated Hook3 protein is a member of a novel family of microtubule-binding proteins. / Walenta, Jason H.; Didier, Aaron J.; Liu, Xinran; Krämer, Helmut.

In: Journal of Cell Biology, Vol. 152, No. 5, 05.03.2001, p. 923-934.

Research output: Contribution to journalArticle

Walenta, Jason H. ; Didier, Aaron J. ; Liu, Xinran ; Krämer, Helmut. / The Golgi-associated Hook3 protein is a member of a novel family of microtubule-binding proteins. In: Journal of Cell Biology. 2001 ; Vol. 152, No. 5. pp. 923-934.
@article{2a4baf43ae9846c1a37876b4c1b73a84,
title = "The Golgi-associated Hook3 protein is a member of a novel family of microtubule-binding proteins",
abstract = "Microtubules are central to the spatial organization of diverse membrane- trafficking systems. Here, we report that Hook proteins constitute a novel family of cytosolic coiled coil proteins that bind to organelles and to microtubules. The conserved NH2-terminal domains of Hook proteins mediate attachment to microtubules, whereas the more divergent COOH-terminal domains mediate the binding to organelles. Human Hook3 bound to Golgi membranes in vitro and was enriched in the cis-Golgi in vivo. Unlike other cis-Golgi-associated proteins, however, a large fraction of Hook3 maintained its juxtanuclear localization after Brefeldin A treatment, indicating a Golgi-independent mechanism for Hook3 localization. Because overexpression of Hook3 caused fragmentation of the Golgi complex, we propose that Hook3 participates in defining the architecture and localization of the mammalian Golgi complex.",
keywords = "Brefeldin A, Endosomes, Golgi complex, Hook protein, Membrane trafficking",
author = "Walenta, {Jason H.} and Didier, {Aaron J.} and Xinran Liu and Helmut Kr{\"a}mer",
year = "2001",
month = "3",
day = "5",
doi = "10.1083/jcb.152.5.923",
language = "English (US)",
volume = "152",
pages = "923--934",
journal = "Journal of Cell Biology",
issn = "0021-9525",
publisher = "Rockefeller University Press",
number = "5",

}

TY - JOUR

T1 - The Golgi-associated Hook3 protein is a member of a novel family of microtubule-binding proteins

AU - Walenta, Jason H.

AU - Didier, Aaron J.

AU - Liu, Xinran

AU - Krämer, Helmut

PY - 2001/3/5

Y1 - 2001/3/5

N2 - Microtubules are central to the spatial organization of diverse membrane- trafficking systems. Here, we report that Hook proteins constitute a novel family of cytosolic coiled coil proteins that bind to organelles and to microtubules. The conserved NH2-terminal domains of Hook proteins mediate attachment to microtubules, whereas the more divergent COOH-terminal domains mediate the binding to organelles. Human Hook3 bound to Golgi membranes in vitro and was enriched in the cis-Golgi in vivo. Unlike other cis-Golgi-associated proteins, however, a large fraction of Hook3 maintained its juxtanuclear localization after Brefeldin A treatment, indicating a Golgi-independent mechanism for Hook3 localization. Because overexpression of Hook3 caused fragmentation of the Golgi complex, we propose that Hook3 participates in defining the architecture and localization of the mammalian Golgi complex.

AB - Microtubules are central to the spatial organization of diverse membrane- trafficking systems. Here, we report that Hook proteins constitute a novel family of cytosolic coiled coil proteins that bind to organelles and to microtubules. The conserved NH2-terminal domains of Hook proteins mediate attachment to microtubules, whereas the more divergent COOH-terminal domains mediate the binding to organelles. Human Hook3 bound to Golgi membranes in vitro and was enriched in the cis-Golgi in vivo. Unlike other cis-Golgi-associated proteins, however, a large fraction of Hook3 maintained its juxtanuclear localization after Brefeldin A treatment, indicating a Golgi-independent mechanism for Hook3 localization. Because overexpression of Hook3 caused fragmentation of the Golgi complex, we propose that Hook3 participates in defining the architecture and localization of the mammalian Golgi complex.

KW - Brefeldin A

KW - Endosomes

KW - Golgi complex

KW - Hook protein

KW - Membrane trafficking

UR - http://www.scopus.com/inward/record.url?scp=0035809910&partnerID=8YFLogxK

UR - http://www.scopus.com/inward/citedby.url?scp=0035809910&partnerID=8YFLogxK

U2 - 10.1083/jcb.152.5.923

DO - 10.1083/jcb.152.5.923

M3 - Article

C2 - 11238449

AN - SCOPUS:0035809910

VL - 152

SP - 923

EP - 934

JO - Journal of Cell Biology

JF - Journal of Cell Biology

SN - 0021-9525

IS - 5

ER -