ER Cargo Properties Specify a Requirement for COPII Coat Rigidity Mediated by Sec13p

Čopič, Alenka; Latham, Catherine F.; Horlbeck, Max A.; D’Arcangelo, Jennifer G.; Miller, Elizabeth A.

doi:10.1126/science.1215909

Cited by 131 publications

(141 citation statements)

References 42 publications

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“…When SEC13 is mutated, the COPII coat may become too flexible and unable to form transport vesicles containing asymmetrically distributed cargoes such as GPI-anchored proteins that confer opposing curvature. Since mutations in genes encoding proteins involved in GPI remodeling and cargo receptors prevent from concentrating GPI-anchored proteins at ER-exit sites, transport vesicles could be formed even in the absence of SEC13 (81,82). These results also suggest that structural remodeling of GPIanchors is required for the sorting of GPI-anchored proteins into the ER-exit sites.…”

Section: Er-to-golgi Transport Of Gpi-anchored Proteinssupporting

confidence: 55%

“…These mutations are called "bypass-of-sec-thirteen (BST)" mutations. Recently, it was reported that other GPI remodeling genes or other p24 family members, including PER1, TED1, GUP1, ERP1 and ERP2, function as BST genes, and that mutations in these genes suppressed the lethality of sec13∆ cells (81). The relationship between SEC13 and BST genes can be explained as follows.…”

Section: Er-to-golgi Transport Of Gpi-anchored Proteinsmentioning

confidence: 99%

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Potential Roles of GPI-Anchor Remodeling in Protein Trafficking and Raft Association in Mammalian Cells

Fujita

2012

TIGG

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Post-translational modification of proteins with glycosylphosphatidylinositol (GPI) is mediated by a mechanism that is conserved in all eukaryotes. GPI-anchored proteins are characterized by their association with specialized membrane domains called "lipid rafts," and the GPI-anchors are thought to regulate their intracellular trafficking pathways. These characteristics are regulated by the structural properties of GPI-anchors, remodeling enzymes and recognition molecules. The biogenesis of GPI-anchored proteins occurs in the ER, following which they are transported to the plasma membrane via the Golgi apparatus. During transport, the structures of the GPI-anchors are remodeled. In this minireview, the structural remodeling of mammalian GPIanchors and regulation of the transport and localization of GPI-anchored proteins are described.

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Section: Er-to-golgi Transport Of Gpi-anchored Proteinssupporting

confidence: 55%

Section: Er-to-golgi Transport Of Gpi-anchored Proteinsmentioning

confidence: 99%

Potential Roles of GPI-Anchor Remodeling in Protein Trafficking and Raft Association in Mammalian Cells

Fujita

2012

TIGG

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“…Thus, although Sar1 and Sec23/Sec24 may participate in membrane curvature, the majority of membrane bending force likely comes from Sec13/Sec31. Indeed, recent genetic and biochemical experiments support this model: Sec31 likely forms all the contacts needed to make the COPII cage (Fath et al 2007) with Sec13 providing structural rigidity to the cage edge element to overcome the membrane bending energy of a cargo-rich membrane (Copic et al 2012). The fundamental function of vesicles is to ensure directional traffic of protein cargoes, making cargo capture an integral part of coat action.…”

Section: Transport From the Er: Sculpting And Populating A Copii Vesiclementioning

confidence: 93%

Secretory Protein Biogenesis and Traffic in the Early Secretory Pathway

2013

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The secretory pathway is responsible for the synthesis, folding, and delivery of a diverse array of cellular proteins. Secretory protein synthesis begins in the endoplasmic reticulum (ER), which is charged with the tasks of correctly integrating nascent proteins and ensuring correct post-translational modification and folding. Once ready for forward traffic, proteins are captured into ER-derived transport vesicles that form through the action of the COPII coat. COPII-coated vesicles are delivered to the early Golgi via distinct tethering and fusion machineries. Escaped ER residents and other cycling transport machinery components are returned to the ER via COPI-coated vesicles, which undergo similar tethering and fusion reactions. Ultimately, organelle structure, function, and cell homeostasis are maintained by modulating protein and lipid flux through the early secretory pathway. In the last decade, structural and mechanistic studies have added greatly to the strong foundation of yeast genetics on which this field was built. Here we discuss the key players that mediate secretory protein biogenesis and trafficking, highlighting recent advances that have deepened our understanding of the complexity of this conserved and essential process. TABLE OF CONTENTS Abstract 383Introduction 384

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“…Thus, CLCs may contribute to uptake of cargoes that pose particular membranebending challenges. Analogously, Sec13p in COPII-coated vesicles contributes structural rigidity that is required to bend membranes with asymmetric cargo, such as GPI-anchored receptors (36). Two GPCR cargoes (μ-opioid receptor and CXCR4) that require CLCs for endocytosis are modified by ubiquitin, which attracts specific endocytic adaptors to promote uptake by clathrin-coated pits (5,31,37).…”

Section: Clc Depletion From Cell Lines Establishes Selectivity For DImentioning

confidence: 99%

Clathrin light chains’ role in selective endocytosis influences antibody isotype switching

Majeed

Evans

et al. 2016

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

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Clathrin, a cytosolic protein composed of heavy and light chain subunits, assembles into a vesicle coat, controlling receptor-mediated endocytosis. To establish clathrin light chain (CLC) function in vivo, we engineered mice lacking CLCa, the major CLC isoform in B lymphocytes, generating animals with CLC-deficient B cells. In CLCa-null mice, the germinal centers have fewer B cells, and they are enriched for IgA-producing cells. This enhanced switch to IgA production in the absence of CLCa was attributable to increased transforming growth factor β receptor 2 (TGFβR2) signaling resulting from defective endocytosis. Internalization of C-X-C chemokine receptor 4 (CXCR4), but not CXCR5, was affected in CLCa-null B cells, and CLC depletion from cell lines affected endocytosis of the δ-opioid receptor, but not the β2-adrenergic receptor, defining a role for CLCs in the uptake of a subset of signaling receptors. This instance of clathrin subunit deletion in vertebrates demonstrates that CLCs contribute to clathrin’s role in vivo by influencing cargo selectivity, a function previously assigned exclusively to adaptor molecules.

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ER Cargo Properties Specify a Requirement for COPII Coat Rigidity Mediated by Sec13p

Cited by 131 publications

References 42 publications

Potential Roles of GPI-Anchor Remodeling in Protein Trafficking and Raft Association in Mammalian Cells

Potential Roles of GPI-Anchor Remodeling in Protein Trafficking and Raft Association in Mammalian Cells

Secretory Protein Biogenesis and Traffic in the Early Secretory Pathway

Clathrin light chains’ role in selective endocytosis influences antibody isotype switching

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