The vesicle docking protein p115 binds GM130, a cis-Golgi matrix protein, in a mitotically regulated manner

Nobuhiro Nakamura; Martin Lowe; Timothy P. Levine; Catherine Rabouille; Graham Warren

doi:10.1016/S0092-8674(00)80225-1

The vesicle docking protein p115 binds GM130, a cis-Golgi matrix protein, in a mitotically regulated manner

Nobuhiro Nakamura
, Martin Lowe
, Timothy P. Levine
, Catherine Rabouille
, Graham Warren^*

^*Corresponding author for this work

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

322 Citations (Scopus)

Abstract

The docking of transport vesicles with their target membrane is thought to be mediated by p115. We show here that GM130, a cis-Golgi matrix protein, interacts specifically with p115 and so could provide a membrane docking site. Deletion analysis showed that the N-terminus binds to p115, whereas the C-terminus binds to Golgi membranes. Mitotic phosphorylation of GM130 or a peptide derived from the N-terminus prevented binding to p115. The peptide also inhibited the NSF- but not the p97-dependent reassembly of Golgi cisternae from mitotic fragments, unless it was mitotically phosphorylated. Together, these data provide a molecular explanation for the COPI-mediated fragmentation of the Golgi apparatus at the onset of mitosis.

Original language	English
Pages (from-to)	445-455
Number of pages	11
Journal	Cell
Volume	89
Issue number	3
DOIs	https://doi.org/10.1016/S0092-8674(00)80225-1
Publication status	Published - 2 May 1997

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title = "The vesicle docking protein p115 binds GM130, a cis-Golgi matrix protein, in a mitotically regulated manner",

abstract = "The docking of transport vesicles with their target membrane is thought to be mediated by p115. We show here that GM130, a cis-Golgi matrix protein, interacts specifically with p115 and so could provide a membrane docking site. Deletion analysis showed that the N-terminus binds to p115, whereas the C-terminus binds to Golgi membranes. Mitotic phosphorylation of GM130 or a peptide derived from the N-terminus prevented binding to p115. The peptide also inhibited the NSF- but not the p97-dependent reassembly of Golgi cisternae from mitotic fragments, unless it was mitotically phosphorylated. Together, these data provide a molecular explanation for the COPI-mediated fragmentation of the Golgi apparatus at the onset of mitosis.",

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AU - Nakamura, Nobuhiro

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AU - Levine, Timothy P.

AU - Rabouille, Catherine

AU - Warren, Graham

PY - 1997/5/2

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AB - The docking of transport vesicles with their target membrane is thought to be mediated by p115. We show here that GM130, a cis-Golgi matrix protein, interacts specifically with p115 and so could provide a membrane docking site. Deletion analysis showed that the N-terminus binds to p115, whereas the C-terminus binds to Golgi membranes. Mitotic phosphorylation of GM130 or a peptide derived from the N-terminus prevented binding to p115. The peptide also inhibited the NSF- but not the p97-dependent reassembly of Golgi cisternae from mitotic fragments, unless it was mitotically phosphorylated. Together, these data provide a molecular explanation for the COPI-mediated fragmentation of the Golgi apparatus at the onset of mitosis.

UR - https://www.scopus.com/pages/publications/0030953187

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JF - Cell

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The vesicle docking protein p115 binds GM130, a cis-Golgi matrix protein, in a mitotically regulated manner

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