Mapping the interaction between GRASP65 and GM130, components of a protein complex involved in the stacking of Golgi cisternae

Barr, Francis A.; Nakamura, Nobuhiro; Warren, Graham

doi:10.1093/emboj/17.12.3258

Cited by 231 publications

(276 citation statements)

References 37 publications

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“…These matrix proteins are required for normal Golgi morphology. GM130 is a cis-Golgi localized coiled-coil protein targeted to membranes via the peripheral membrane protein GRASP65 (Barr et al, 1997(Barr et al, , 1998. It also binds the vesicle tethering factor p115 (Nakamura et al, 1997;Nelson et al, 1998).…”

Section: Cargo Receptor Silencing Destabilizes the Ergic Without Affementioning

confidence: 99%

The Cargo Receptors Surf4, Endoplasmic Reticulum-Golgi Intermediate Compartment (ERGIC)-53, and p25 Are Required to Maintain the Architecture of ERGIC and Golgi

Mitrović

Ben-Tekaya

Koegler

et al. 2008

MBoC

114

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Rapidly cycling proteins of the early secretory pathway can operate as cargo receptors. Known cargo receptors are abundant proteins, but it remains mysterious why their inactivation leads to rather limited secretion phenotypes. Studies of Surf4, the human orthologue of the yeast cargo receptor Erv29p, now reveal a novel function of cargo receptors. Surf4 was found to interact with endoplasmic reticulum-Golgi intermediate compartment (ERGIC)-53 and p24 proteins. Silencing Surf4 together with ERGIC-53 or silencing the p24 family member p25 induced an identical phenotype characterized by a reduced number of ERGIC clusters and fragmentation of the Golgi apparatus without effect on anterograde transport. Live imaging showed decreased stability of ERGIC clusters after knockdown of p25. Silencing of Surf4/ERGIC-53 or p25 resulted in partial redistribution of coat protein (COP) I but not Golgi matrix proteins to the cytosol and partial resistance of the cis-Golgi to brefeldin A. These findings imply that cargo receptors are essential for maintaining the architecture of ERGIC and Golgi by controlling COP I recruitment. INTRODUCTIONThe secretory pathway of higher eukaryotic cells is composed of the three membrane organelles endoplasmic reticulum (ER), ER-Golgi intermediate compartment (ERGIC), and Golgi (Bonifacino and Glick, 2004;Appenzeller-Herzog and Hauri, 2006). Maintenance of these organelles requires a balance of anterograde (secretory) and retrograde vesicular traffic. Anterograde traffic from ER to ERGIC is mediated by coat protein (COP) II vesicles that form at ER exit sites (Aridor et al., 1995;Zeuschner et al., 2006) and fuse with the ERGIC that consists of a few hundred tubulovesicular membrane clusters in vicinity of ER exit sites (AppenzellerHerzog and Hauri, 2006). Transport from ERGIC to Golgi is mediated by pleomorphic vesicles (Ben-Tekaya et al., 2005) that carry COP I (Presley et al., 1997;Scales et al., 1997), although the mechanism of their formation remains unknown. Retrograde traffic mediated by COP I vesicles can occur from ERGIC or Golgi and recycles membrane proteins that possess either dilysine signals, including ERGIC-53 and KDEL-receptor, or diphenylalanine signals, such as members of the 24 protein family. This rapid COP I-dependent recycling is distinct from the slow Golgi-to-ER recycling of Golgi resident proteins that is COP I independent and can be either constitutive or induced (Storrie, 2005).Major constituents of anterograde and retrograde transport vesicles are transmembrane cargo receptors that mediate protein sorting by linking soluble cargo on the luminal side and coat assembly on the cytoplasmic side. To date, only few cargo receptors have been studied in detail. The polytopic transmembrane protein Erv29p is known to cycle between ER and Golgi in yeast and to operate as a cargo receptor (Belden and Barlowe, 2001). Erv29p is required for efficient packaging of the glycosylated ␣-factor pheromone precursor into COP II vesicles departing from the ER. Maturation of carboxypeptidase Y...

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Section: Cargo Receptor Silencing Destabilizes the Ergic Without Affementioning

confidence: 99%

The Cargo Receptors Surf4, Endoplasmic Reticulum-Golgi Intermediate Compartment (ERGIC)-53, and p25 Are Required to Maintain the Architecture of ERGIC and Golgi

Mitrović

Ben-Tekaya

Koegler

et al. 2008

MBoC

114

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“…Pioneering functional reconstitution studies using a cell-free system in which Golgi stacks (but not ribbons) reassemble from mitotic extracts (5-8) yielded two classes of purified proteins, each clearly contributing to stacking: globular Golgi reassembly and stacking proteins (GRASPs; the homologous proteins GRASP65 and GRASP55) (7,9) and the helical rod-like and partially homologous proteins Golgi matrix protein of 130 kDa (GM130) and Golgin of 45 kDa (Golgin45) (10,11). One member of each family (GRASP65 and GM130) is located in the cis-most cisterna (7,12), and another member of each family (GRASP55 and Golgin45) is located in this (and more so in later cisternae) (9,10).…”

mentioning

confidence: 99%

“…One member of each family (GRASP65 and GM130) is located in the cis-most cisterna (7,12), and another member of each family (GRASP55 and Golgin45) is located in this (and more so in later cisternae) (9,10). The GRASP proteins bind to the Golgins (note that we use the term "Golgin" in a limited sense in this article to refer either to GM130 or Golgin45) (10,11). An appealing mechanism for intercisternal adhesion has been proposed for the GRASP proteins based on X-ray crystallography and biochemistry that involves PSD-95, Dlg1, Zo-1 domain-dependent homo-oligomerization in trans (13)(14)(15).…”

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confidence: 99%

Membrane adhesion dictates Golgi stacking and cisternal morphology

Lee

Tiwari

Dunlop

et al. 2014

Proc. Natl. Acad. Sci. U.S.A.

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Two classes of proteins that bind to each other and to Golgi membranes have been implicated in the adhesion of Golgi cisternae to each other to form their characteristic stacks: Golgi reassembly and stacking proteins 55 and 65 (GRASP55 and GRASP65) and Golgin of 45 kDa and Golgi matrix protein of 130 kDa. We report here that efficient stacking occurs in the absence of GRASP65/55 when either Golgin is overexpressed, as judged by quantitative electron microscopy. The Golgi stacks in these GRASP-deficient HeLa cells were normal both in morphology and in anterograde cargo transport. This suggests the simple hypothesis that the total amount of adhesive energy gluing cisternae dictates Golgi cisternal stacking, irrespective of which molecules mediate the adhesive process. In support of this hypothesis, we show that adding artificial adhesive energy between cisternae and mitochondria by dimerizing rapamycin-binding domain and FK506-binding protein domains that are attached to cisternal adhesive proteins allows mitochondria to invade the stack and even replace Golgi cisternae within a few hours. These results indicate that although Golgi stacking is a highly complicated process involving a large number of adhesive and regulatory proteins, the overriding principle of a Golgi stack assembly is likely to be quite simple. From this simplified perspective, we propose a model, based on cisternal adhesion and cisternal maturation as the two core principles, illustrating how the most ancient form of Golgi stacking might have occurred using only weak cisternal adhesive processes because of the differential between the rate of influx and outflux of membrane transport through the Golgi.tethers | GRASPs T he Golgi apparatus plays a central role in the processing, sorting, and secretion of various cargo molecules destined for various intracellular and extracellular destinations (1). In animal and plant cells, its unique structure of four to six stacked, roughly planar cisternae serves, among other things, as a platform to organize Golgi resident glycosyltransferases into distinct membrane-bound subcompartments (the cis-, medial-, and trans-Golgi cisternae) for proper and sequential posttranslational maturation of the transiting cargo proteins (2, 3).Although these characteristic features of Golgi morphology have drawn the attention of many researchers for many decades, the molecular mechanisms underlying them are still unclear (4). Pioneering functional reconstitution studies using a cell-free system in which Golgi stacks (but not ribbons) reassemble from mitotic extracts (5-8) yielded two classes of purified proteins, each clearly contributing to stacking: globular Golgi reassembly and stacking proteins (GRASPs; the homologous proteins GRASP65 and GRASP55) (7, 9) and the helical rod-like and partially homologous proteins Golgi matrix protein of 130 kDa (GM130) and Golgin of 45 kDa (Golgin45) (10, 11). One member of each family (GRASP65 and GM130) is located in the cis-most cisterna (7, 12), and another member of each family (GRASP5...

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“…In an effort to identify components required for post-mitotic reassembly of Golgi cisternae, a peripheral Golgi protein termed GRASP65 (Golgi reassembly stacking protein of 65 kDa) was identified (5). GRASP65 localizes to the cis-Golgi through its N-terminal myristoylation and interaction with GM130, a cis-Golgi marker (6,7). Modification of GRASP65 on mitotic Golgi fragments by N-ethylmaleimide in vitro and the microinjection of antibodies against GRASP65 into mitotic cells inhibit the stacking of reformed Golgi cisternae (5,8).…”

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confidence: 99%

Structural Insight into Golgi Membrane Stacking by GRASP65 and GRASP55 Proteins

Feng

et al. 2013

Journal of Biological Chemistry

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Background:The oligomerization of GRASP65 and GRASP55 is required to tether Golgi membranes. Results: The crystal structures reveal two types of intermolecular interactions, and biochemical and cellular assays confirm these observations. Conclusion: Two relatively weak interactions in combination are needed for GRASP-mediated Golgi stacking. Significance: These data suggest a novel mode of Golgi membrane stacking by the GRASP proteins.

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Mapping the interaction between GRASP65 and GM130, components of a protein complex involved in the stacking of Golgi cisternae

Cited by 231 publications

References 37 publications

The Cargo Receptors Surf4, Endoplasmic Reticulum-Golgi Intermediate Compartment (ERGIC)-53, and p25 Are Required to Maintain the Architecture of ERGIC and Golgi

The Cargo Receptors Surf4, Endoplasmic Reticulum-Golgi Intermediate Compartment (ERGIC)-53, and p25 Are Required to Maintain the Architecture of ERGIC and Golgi

Membrane adhesion dictates Golgi stacking and cisternal morphology

Structural Insight into Golgi Membrane Stacking by GRASP65 and GRASP55 Proteins

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