TY - JOUR
T1 - The vesicle docking protein p115 binds GM130, a cis-Golgi matrix protein, in a mitotically regulated manner
AU - Nakamura, Nobuhiro
AU - Lowe, Martin
AU - Levine, Timothy P.
AU - Rabouille, Catherine
AU - Warren, Graham
PY - 1997/5/2
Y1 - 1997/5/2
N2 - 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.
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 - http://www.scopus.com/inward/record.url?scp=0030953187&partnerID=8YFLogxK
U2 - 10.1016/S0092-8674(00)80225-1
DO - 10.1016/S0092-8674(00)80225-1
M3 - Article
C2 - 9150144
AN - SCOPUS:0030953187
SN - 0092-8674
VL - 89
SP - 445
EP - 455
JO - Cell
JF - Cell
IS - 3
ER -