Coordinated regulation of bidirectional COPI transport at the Golgi by CDC42

Park, Seung-Yeol; Yang, Jia‐Shu; Schmider, Angela B.; Soberman, Roy J.; Hsu, Victor

doi:10.1038/nature14457

Cited by 76 publications

(100 citation statements)

References 25 publications

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“…A C-terminal valine residue, which is common in type I membrane proteins, has also been proposed to serve as an anterograde signal by associating with Golgi matrix proteins (GRASP65 and -55) (D'Angelo et al 2009). Finally, COPI acting in concert with CDC42 may promote forward transport in the Golgi complex by targeting cargo to tubular Golgi elements (Park et al 2015).…”

Section: Retrograde Sorting Signals and Receptorsmentioning

confidence: 99%

Cargo Capture and Bulk Flow in the Early Secretory Pathway

Barlowe

Helenius

2016

Annu. Rev. Cell Dev. Biol.

175

191

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Transport of newly synthesized proteins from the endoplasmic reticulum (ER) to the Golgi complex is highly selective. As a general rule, such transport is limited to soluble and membrane-associated secretory proteins that have reached properly folded and assembled conformations. To secure the efficiency, fidelity, and control of this crucial transport step, cells use a combination of mechanisms. The mechanisms are based on selective retention of proteins in the ER to prevent uptake into transport vesicles, on selective capture of proteins in COPII carrier vesicles, on inclusion of proteins in these vesicles by default as part of fluid and membrane bulk flow, and on selective retrieval of proteins from post-ER compartments by retrograde vesicle transport.

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Section: Retrograde Sorting Signals and Receptorsmentioning

confidence: 99%

Cargo Capture and Bulk Flow in the Early Secretory Pathway

Barlowe

Helenius

2016

Annu. Rev. Cell Dev. Biol.

175

191

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“…Following up on this discovery, a recent study has found that Cdc42 not only inhibits the sorting of retrograde cargoes into COPI vesicles, but also promotes the formation of COPI tubules to enhance anterograde Golgi transport [24]. Although vesicle and tubule formation are both initiated by the formation of COPI buds from Golgi membrane, vesicle formation involves the subsequent constriction of the bud neck that eventually results in vesicles being released from organellar membrane, a process known as vesicle fission.…”

Section: The Golgi Pool Acts Independently Of the Plasma Membrane Poolmentioning

confidence: 99%

Cdc42 and Cellular Polarity: Emerging Roles at the Golgi

Farhan

Hsu

2016

Trends in Cell Biology

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Cdc42 belongs to the Rho family of small GTPases and plays key roles in cellular events of polarity. This role of Cdc42 has typically been attributed to its function at the plasma membrane. However, Cdc42 also exists at the Golgi complex. In this review, we summarize major insights that have been gathered in studying the Golgi-pool of Cdc42 and propose that Golgi-localized Cdc42 enables the cell to diversify the function of Cdc42, which in some cases represent new roles, and in other cases act to complement the established roles of Cdc42 at the plasma membrane. Studies on how Cdc42 acts at the Golgi also suggest key questions to address in the future.

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“…This observation suggests that the DxE motif in the cytosolic tail, in addition to being responsible for VSVG recruitment to ERES (Nishimura and Balch, 1997;Sevier et al, 2000), also plays a role in driving the progression of VSVG through the Golgi. Recently, five basic residues upstream of the DxE motif have been shown to favor the transport of VSVG through the Golgi through a COPI-CDC42-regulated pathway (Park et al, 2015).…”

Section: Lipid-dependent Sortingmentioning

confidence: 99%

Getting membrane proteins on and off the shuttle bus between the endoplasmic reticulum and the Golgi complex

Borgese

2016

Journal of Cell Science

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Secretory proteins exit the endoplasmic reticulum (ER) in coat protein complex II (COPII)-coated vesicles and then progress through the Golgi complex before delivery to their final destination. Soluble cargo can be recruited to ER exit sites by signal-mediated processes (cargo capture) or by bulk flow. For membrane proteins, a third mechanism, based on the interaction of their transmembrane domain (TMD) with lipid microdomains, must also be considered. In this Commentary, I review evidence in favor of the idea that partitioning of TMDs into bilayer domains that are endowed with distinct physico-chemical properties plays a pivotal role in the transport of membrane proteins within the early secretory pathway. The combination of such selforganizational phenomena with canonical intermolecular interactions is most likely to control the release of membrane proteins from the ER into the secretory pathway.

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Coordinated regulation of bidirectional COPI transport at the Golgi by CDC42

Cited by 76 publications

References 25 publications

Cargo Capture and Bulk Flow in the Early Secretory Pathway

Cargo Capture and Bulk Flow in the Early Secretory Pathway

Cdc42 and Cellular Polarity: Emerging Roles at the Golgi

Getting membrane proteins on and off the shuttle bus between the endoplasmic reticulum and the Golgi complex

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