The Golgi matrix protein GM130: a specific interacting partner of the small GTPase rab1b

Weide, Thomas; Bayer, Michael; Köster, M.; Siebrasse, Jan Peter; Peters, Reiner; Barnekow, Angelika

doi:10.1093/embo-reports/kve065

Cited by 115 publications

(100 citation statements)

References 35 publications

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“…p115 Regulates the GM130-Rab1 Interaction-In addition to p115 and syntaxin 5, GM130 can also interact with the small GTPase Rab1 (15,16). Rab1 binds to GM130 via a central coiled-coil region (coiled-coil 3) that lies downstream from the N-terminal p115 binding site (16).…”

Section: Resultsmentioning

confidence: 99%

“…Rab1 binds to GM130 via a central coiled-coil region (coiled-coil 3) that lies downstream from the N-terminal p115 binding site (16). Since p115 binding to GM130 could influence the distal binding of syntaxin 5, most likely through an induced conformational change, we decided to test whether it could also influence GM130 binding to Rab1.…”

Section: Resultsmentioning

confidence: 99%

“…The syntaxin 5 binding site was mapped to a C-terminal region encompassing coiled-coils 4 -6, which is distinct from the interaction sites of other proteins, which bind either to the extreme N terminus (p115), coiled-coil 1 (YSK1), coiled-coil 3 (Rab1), or the extreme C terminus (GRASP65) of the protein (9,10,16,41). An obvious concern is that the binding between GM130 and syntaxin 5 is nonspecific, simply reflecting the stabilization of the ␣-helical SNARE motif in syntaxin 5 by the coiled-coil regions of GM130.…”

Section: Discussionmentioning

confidence: 99%

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Coordination of Golgin Tethering and SNARE Assembly

Diao

Frost

Morohashi

et al. 2008

Journal of Biological Chemistry

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During membrane traffic, transport carriers are first tethered to the target membrane prior to undergoing fusion. Mechanisms exist to connect tethering with fusion, but in most cases, the details remain poorly understood. GM130 is a member of the golgin family of coiled-coil proteins that is involved in membrane tethering at the endoplasmic reticulum (ER) to Golgi intermediate compartment and cis-Golgi. Here, we demonstrate that GM130 interacts with syntaxin 5, a t-SNARE also localized to the early secretory pathway. Binding to syntaxin 5 is specific, direct, and mediated by the membrane-proximal region of GM130. Interestingly, interaction with syntaxin 5 is inhibited by the binding of the vesicle docking protein p115 to a distal binding site in GM130. The interaction between GM130 and the small GTPase Rab1 is also inhibited by p115 binding. Our findings suggest a mechanism for coupling membrane tethering and fusion at the ER to Golgi intermediate compartment and cis-Golgi, with GM130 playing a central role in linking these processes. Consistent with this hypothesis, we find that depletion of GM130 by RNA interference slows the rate of ER to Golgi trafficking in vivo. The interactions of GM130 with syntaxin 5 and Rab1 are also regulated by mitotic phosphorylation, which is likely to contribute to the inhibition of ER to Golgi trafficking that occurs when mammalian cells enter mitosis.

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Section: Resultsmentioning

confidence: 99%

Section: Resultsmentioning

confidence: 99%

Section: Discussionmentioning

confidence: 99%

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Coordination of Golgin Tethering and SNARE Assembly

Diao

Frost

Morohashi

et al. 2008

Journal of Biological Chemistry

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“…A resolution for these discrepancies might be related to the function of Rab1, which also acts during ER to Golgi and intra-Golgi transport and binds directly to p115 and golgin tethering proteins (41)(42)(43). Rab family GTPases function throughout the exocytic pathway and several family members are implicated in tethering (4,6,7,44).…”

mentioning

confidence: 99%

“…Rab proteins undergo a cycle of GTP binding and hydrolysis that switches between their active and inactive states, respectively. In the active state they bind effectors that are either membrane proteins (43,45,46) or that become recruited to membranes by the Rab itself (41,47). After GTP hydrolysis, Rab proteins are removed from the membrane by Rab-GDP dissociation inhibitor.…”

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confidence: 99%

A Cryptic Rab1-binding Site in the p115 TetheringProtein

Beard

Satoh

Shorter

et al. 2005

Journal of Biological Chemistry

103

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Small GTPases and coiled-coil proteins of the golgin family help to tether COPI vesicles to Golgi membranes. At the cis-side of the Golgi, the Rab1 GTPase binds directly to each of three coiled-coil proteins: p115, GM130, and as now shown, Giantin. Rab1 binds to a coiled-coil region within the tail domain of p115 and this binding is inhibited by the C-terminal, acidic domain of p115. Furthermore, GM130 and Giantin bind to the acidic domain of p115 and stimulate p115 binding to Rab1, suggesting that p115 binding to Rab1 is regulated. Regulation of this interaction by proteins such as GM130 and Giantin may control the membrane recruitment of p115 by Rab1.

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The TRAPP complexes: oligomeric exchange factors that activate the small GTPases Rab1 and Rab11

Galindo

Munro

2022

FEBS Letters

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The Transport Protein Particle (TRAPP) complexes are highly conserved multisubunit complexes that act as nucleotide exchange factors (GEFs) for Rab GTPases. They act in both protein secretion and autophagy and have also been proposed to have a role in other processes such as cytokinesis and ciliogenesis. There are two TRAPP complexes in metazoans: TRAPPII, which activates Rab11; and TRAPPIII, which activates Rab1. Both complexes share a core of small subunits that form the active site for the exchange of GDP for GTP. In addition, each TRAPP complex has distinct large subunits that determine the specificity of each complex towards its substrate Rab and are essential for activity in vivo. Crystal structures have revealed the organisation of the TRAPP core and the mechanism of Rab1 activation, whilst recent cryo‐EM structures have unveiled the arrangement of the specific subunits around the core to form each complex. Combining these findings with functional experiments has allowed the proposal of mechanisms for how the specificity of each complex towards their cognate Rab is determined and for the arrangement of these large complexes on the membrane.

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The Golgi matrix protein GM130: a specific interacting partner of the small GTPase rab1b

Cited by 115 publications

References 35 publications

Coordination of Golgin Tethering and SNARE Assembly

Coordination of Golgin Tethering and SNARE Assembly

A Cryptic Rab1-binding Site in the p115 TetheringProtein

The TRAPP complexes: oligomeric exchange factors that activate the small GTPases Rab1 and Rab11

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