The endoplasmic reticulum (ER) is considered a prominent membrane source for the formation of autophagosomes. Recent results from our laboratory revealed a cellular mechanism for the contribution of the ER to autophagosomes in yeast: membranes, together with unconventional membrane fusion machinery, are delivered to sites of autophagosome formation by specific coat protein complex II (COPII) vesicles.
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| http://dx.doi.org/10.1080/23723556.2016.1173768 | DOI Listing |
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Newly synthesized proteins destined for the secretory pathway are folded and assembled in the endoplasmic reticulum (ER) and then transported to the Golgi apparatus via COPII vesicles, which are normally 60-90 nm. COPII vesicles must accordingly be enlarged to accommodate proteins larger than 90 nm, such as long-chain collagen. Key molecules involved in this enlargement are Tango1 and Tango1-like (Tali), which are transmembrane proteins in the ER encoded by the MIA3 and MIA2 genes, respectively.
View Article and Find Full Text PDFMultifunctional Roles of Sec13 Paralogues in the Euglenozoan .
bioRxiv
December 2024
Department of Microbiology and Immunology, Jacobs School of Medicine and Biomedical Sciences, University at Buffalo, 955 Main Street, Buffalo NY 14203.
Secretory cargos are exported from the ER via COPII coated vesicles that have an inner matrix of Sec23/Sec24 heterotetramers and an outer cage of Sec13/Sec31 heterotetramers. In addition to COPII, Sec13 is part of the nuclear pore complex (NPC) and the regulatory SEA/GATOR complex in eukaryotes, which typically have one Sec13 orthologue. The kinetoplastid parasite has two paralogues: TbSec13.
View Article and Find Full Text PDFER export via SURF4 uses diverse mechanisms of both client and coat engagement.
J Cell Biol
January 2025
MRC Laboratory of Molecular Biology , Cambridge, UK.
Protein secretion is an essential process that drives cell growth and communication. Enrichment of soluble secretory proteins into ER-derived transport carriers occurs via transmembrane cargo receptors that connect lumenal cargo to the cytosolic COPII coat. Here, we find that the cargo receptor, SURF4, recruits different SEC24 cargo adaptor paralogs of the COPII coat to export different cargoes.
View Article and Find Full Text PDFTMEM39A and TMEM131 facilitate bulk transport of ECM proteins through large COPII vesicle formation.
J Genet Genomics
November 2024
Cancer Metastasis Branch, Research Institute, National Cancer Center, 323 Ilsan-ro, Goyang-si, Gyeonggi-do, 10408, Republic of Korea. Electronic address:
The growth of Caenorhabditis elegans involves multiple molting processes, during which old cuticles are shed and new cuticles are rapidly formed. This process requires the regulated bulk secretion of cuticle components. The transmembrane protein-39 (TMEM-39) mutant exhibits distinct dumpy and ruptured phenotypes characterized by notably thin cuticles.
View Article and Find Full Text PDFCryo-electron tomography reveals how COPII assembles on cargo-containing membranes.
Nat Struct Mol Biol
November 2024
Institute of Structural and Molecular Biology, Birkbeck College, London, UK.
Proteins traverse the eukaryotic secretory pathway through membrane trafficking between organelles. The coat protein complex II (COPII) mediates the anterograde transport of newly synthesized proteins from the endoplasmic reticulum, engaging cargoes with a wide range of size and biophysical properties. The native architecture of the COPII coat and how cargo might influence COPII carrier morphology remain poorly understood.
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