Vesicle coats: structure, function, and general principles of assembly

Faini, Marco; Beck, Rainer; Wieland, Felix; Briggs, John

doi:10.1016/j.tcb.2013.01.005

Cited by 160 publications

(145 citation statements)

References 79 publications

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“…11), which led us to hypothesize that they share a common evolutionary ancestor termed the “protocoatomer” 34 . Two major families of coating complexes exist: COPI/clathrin and COPII, with each having discrete vesicle recognition and trafficking roles 35,36 . We find both COPI/clathrin-like and COPII-like features in the NPC, suggesting that ancestral COPI and COPII coating families evolved first, followed by the NPC, which may have evolved through a partnership of COPI and COPII coats.…”

Section: Resultsmentioning

confidence: 99%

Integrative structure and functional anatomy of a nuclear pore complex

Kim

Fernández-Martı́nez

Nudelman

et al. 2018

Nature

480

894

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Summary Despite the central role of Nuclear Pore Complexes (NPCs) as gatekeepers of RNA and protein transport between the cytoplasm and nucleoplasm, their large size and dynamic nature have impeded a full structural and functional elucidation. Here, we have determined a subnanometer precision structure for the entire 552-protein yeast NPC by satisfying diverse data including stoichiometry, a cryo-electron tomography map, and chemical cross-links. The structure reveals the NPC’s functional elements in unprecedented detail. The NPC is built of sturdy diagonal columns to which are attached connector cables, imbuing both strength and flexibility, while tying together all other elements of the NPC, including membrane-interacting regions and RNA processing platforms. Inwardly-directed anchors create a high density of transport factor-docking Phe-Gly repeats in the central channel, organized in distinct functional units. Taken together, this integrative structure allows us to rationalize the architecture, transport mechanism, and evolutionary origins of the NPC.

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Section: Resultsmentioning

confidence: 99%

Integrative structure and functional anatomy of a nuclear pore complex

Kim

Fernández-Martı́nez

Nudelman

et al. 2018

Nature

480

894

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“…Dual role of Bic-D in stimulating endocytosis at the posterior pole of the oocyte Chc is the main structural component of clathrin-coated pits and vesicles, and a central player in clathrin-mediated endocytosis (Brodsky, 2012;Faini et al, 2013). The association of Bic-D with Chc led us to discover that Bic-D is needed for endocytosis in the oocyte through two different mechanisms.…”

Section: Discussionmentioning

confidence: 99%

Clathrin heavy chain plays multiple roles in polarizing the Drosophila oocyte downstream of Bic-D

et al. 2014

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Bicaudal-D (Bic-D), Egalitarian (Egl), microtubules and their motors form a transport machinery that localizes a remarkable diversity of mRNAs to specific cellular regions during oogenesis and embryogenesis. Bic-D family proteins also promote dynein-dependent transport of Golgi vesicles, lipid droplets, synaptic vesicles and nuclei. However, the transport of these different cargoes is still poorly understood. We searched for novel proteins that either mediate Bic-Ddependent transport processes or are transported by them. Clathrin heavy chain (Chc) co-immunopurifies with Bic-D in embryos and ovaries, and a fraction of Chc colocalizes with Bic-D. Both proteins control posterior patterning of the Drosophila oocyte and endocytosis. Although the role of Chc in endocytosis is well established, our results show that Bic-D is also needed for the elevated endocytic activity at the posterior of the oocyte. Apart from affecting endocytosis indirectly by its role in osk mRNA localization, Bic-D is also required to transport Chc mRNA into the oocyte and for transport and proper localization of Chc protein to the oocyte cortex, pointing to an additional, more direct role of Bic-D in the endocytic pathway. Furthermore, similar to Bic-D, Chc also contributes to proper localization of osk mRNA and to oocyte growth. However, in contrast to other endocytic components and factors of the endocytic recycling pathway, such as Rabenosyn-5 (Rbsn-5) and Rab11, Chc is needed during early stages of oogenesis (from stage 6 onwards) to localize osk mRNA correctly. Moreover, we also uncovered a novel, presumably endocytosis-independent, role of Chc in the establishment of microtubule polarity in stage 6 oocytes.

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“…COPI-dependent retrograde transport has been investigated in great detail, as reviewed recently (Faini et al, 2013;Spang, 2013;Jackson, 2014). As in the case of COPII vesicles, the COPI heptamer is recruited to the Golgi membrane by a small GTPase (Arf1), and has the dual function of bending the membrane and of binding to cargo proteins or receptors through recognition of discrete sorting signals on their cytosolic tails (Jackson et al, 1990;Cosson et al, 1998; reviewed in Dancourt and Barlowe, 2010).…”

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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Vesicle coats: structure, function, and general principles of assembly

Cited by 160 publications

References 79 publications

Integrative structure and functional anatomy of a nuclear pore complex

Integrative structure and functional anatomy of a nuclear pore complex

Clathrin heavy chain plays multiple roles in polarizing the Drosophila oocyte downstream of Bic-D

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

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