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Lysophospholipids Facilitate COPII Vesicle Formation [PDF]
Current Biology, 2018 Coat protein complex II (COPII) proteins form vesicles from the endoplasmic reticulum to export cargo molecules to the Golgi apparatus. Among the many proteins involved in this process, Sec12 is a key regulator, functioning as the guanosine diphosphate (GDP) exchange factor for Sar1p, the small guanosine triphosphatase (GTPase) that initiates COPII ...
Alejandro Melero +2 more
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COPII-mediated traffic in plants
Trends in Plant Science, 2010The secretory pathway encloses functionally interlinked organelles for the synthesis and deposition of most of the building blocks of eukaryotic cells, such as lipids, proteins and sugars. The coat protein complex II (COPII) is a specialized protein complex for the transport between secretory organelles, specifically from the endoplasmic reticulum (ER)
MARTI, LUCIA +4 more
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Role of Rab1b in COPII dynamics and function
European Journal of Cell Biology, 2011 In eukaryotic cells, proteins destined for secretion are translocated into the endoplasmic reticulum (ER) and packaged into so-called COPII-coated vesicles. In the ER exit sites (ERES), COPII has the capacity of deforming the lipid bilayer, where it modulates the selective sorting and concentration of cargo proteins.
Pablo Monetta, Cecilia Alvarez
exaly +3 more sources
A unique COPII population in plant autophagy
Autophagy, 2021Increasing evidence supports the bona fide function of the coat protein complex II (COPII) machinery in regulating autophagosomes biogenesis during macroautophagy/autophagy induced by nutrient starvation. However, the participation of the COPII machinery in the plant autophagy pathway remains elusive. We recently identified a unique population of COPII
Yonglun, Zeng, Liwen, Jiang
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Molecular mechanisms of COPII vesicle formation
Seminars in Cell & Developmental Biology, 2007The first step in protein secretion from eukaryotic cells is mediated by COPII vesicles, known for the cytoplasmic coat proteins that are the minimal machinery required to generate these small transport carriers. The five COPII coat components coordinate to create a vesicle by locally generating membrane curvature and populating the incipient bud with ...
Lee, Marcus C.S., Miller, Elizabeth A.
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Multifaceted roles of COPII subunits in autophagy
Biochimica Et Biophysica Acta - Molecular Cell Research, 2020 COPII vesicles mediate anterograde ER-Golgi traffic of newly synthesized proteins in nutrient rich conditions. An accumulating body of results indicates that the secretory COPII vesicles can be shifted to the roles in autophagosome formation and selective ER-phagy (autophagy of ER), depending on their specific subunits, in response to environmental ...
Zhongyu, Li, Wei, Huang, Wei, Wang
exaly +3 more sources
COPII-mediated vesicle formation at a glance
Journal of Cell Science, 2011Eukaryotic cells contain a number of different membrane compartments that have specialized roles. Each compartment depends on a specific mixture of proteins for its identity and function. For many compartments, proteins arrive by way of small membrane vesicles that travel through the cell from ...
Devon, Jensen, Randy, Schekman
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Coordination of COPII vesicle trafficking by Sec23
Trends in Cell Biology, 2008Coat protein complex II (COPII) is a multi-subunit protein complex responsible for the formation of membrane vesicles at the endoplasmic reticulum. The assembly of this complex on the endoplasmic reticulum membrane needs to be tightly regulated to ensure efficient and specific incorporation of cargo proteins into nascent vesicles.
J Christopher, Fromme +2 more
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1999
Abstract Genes encoding COPII proteins were first identified inS. cerevisiae through a genetic screen for secretion defective cells and later found to be required for transport vesicle budding from the ER. Subsequent biochemical approaches allowed for the isolation of three protein fractions, Sec23p/Sec24p complex, Sec13p/Sec31p, and ...
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Abstract Genes encoding COPII proteins were first identified inS. cerevisiae through a genetic screen for secretion defective cells and later found to be required for transport vesicle budding from the ER. Subsequent biochemical approaches allowed for the isolation of three protein fractions, Sec23p/Sec24p complex, Sec13p/Sec31p, and ...
openaire +1 more source
1962
Abstract : The upper portion of core from approximately 75400B to 77777B is now used by the COPII (Control for Operational Programs) System for the directory and other tables. Some functions in the system either require all of core from 10000B to 77777B or are very close to requiring the area now used for the directory.
J.B. Munson, B.R. Pruett
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Abstract : The upper portion of core from approximately 75400B to 77777B is now used by the COPII (Control for Operational Programs) System for the directory and other tables. Some functions in the system either require all of core from 10000B to 77777B or are very close to requiring the area now used for the directory.
J.B. Munson, B.R. Pruett
openaire +1 more source