The GM130 and GRASP65 Golgi proteins cycle through and define a subdomain of the intermediate compartment
- 9 November 2001
- journal article
- research article
- Published by Springer Science and Business Media LLC in Nature
- Vol. 3 (12), 1101-1113
- https://doi.org/10.1038/ncb1201-1101
Abstract
Integrating the pleomorphic membranes of the intermediate compartment (IC) into the array of Golgi cisternae is a crucial step in membrane transport, but it is poorly understood. To gain insight into this step, we investigated the dynamics by which cis-Golgi matrix proteins such as GM130 and GRASP65 associate with, and incorporate, incoming IC elements. We found that GM130 and GRASP65 cycle via membranous tubules between the Golgi complex and a constellation of mobile structures that we call late IC stations. These stations are intermediate between the IC and the cis-Golgi in terms of composition, and they receive cargo from earlier IC elements and deliver it to the Golgi complex. Late IC elements are transient in nature and sensitive to fixatives; they are seen in only a fraction of fixed cells, whereas they are always visible in living cells. Finally, late IC stations undergo homotypic fusion and establish tubular connections between themselves and the Golgi. Overall, these features indicate that late IC stations mediate the transition between IC elements and the cis-Golgi face.This publication has 49 references indexed in Scilit:
- The membrane transport factor p115 recycles only between homologous compartments in intact heterokaryonsEuropean Journal of Cell Biology, 2000
- ER to Golgi TransportThe Journal of cell biology, 1999
- Localization, Dynamics, and Protein Interactions Reveal Distinct Roles for ER and Golgi SNAREsThe Journal of cell biology, 1998
- GRASP65, a Protein Involved in the Stacking of Golgi CisternaeCell, 1997
- Isolation of a matrix that binds medial Golgi enzymesThe Journal of cell biology, 1994
- Characterization of the budding compartment of mouse hepatitis virus: evidence that transport from the RER to the Golgi complex requires only one vesicular transport stepThe Journal of cell biology, 1994
- Molecular characterization of two human autoantigens: unique cDNAs encoding 95- and 160-kD proteins of a putative family in the Golgi complex.The Journal of Experimental Medicine, 1993
- Immunocytochemical analysis of the transfer of vesicular stomatitis virus G glycoprotein from the intermediate compartment to the Golgi complex.The Journal of cell biology, 1992
- The Golgi complex: In vitro veritas?Cell, 1992
- Movement of internalized ligand–receptor complexes along a continuous endosomal reticulumNature, 1990