COPII and secretory cargo capture into transport vesicles.

نویسندگان

  • M J Kuehn
  • R Schekman
چکیده

Yeast cylosolic coat proteins (COPII) direct the formation of vesicles from the endoplasmic reticulum. The vesicles selectively capture both cargo molecules and the secretory machinery that is necessary for the fusion of the vesicle with the recipient compartment, the Golgi apparatus. Recent efforts have aimed to understand how proteins are selected for inclusion into these vesicles. A variety of cargo adaptors may concentrate and sort secretory and membrane proteins by direct or indirect interaction with a subset of coat protein subunits.

منابع مشابه

Sar1p N-Terminal Helix Initiates Membrane Curvature and Completes the Fission of a COPII Vesicle

Secretory proteins traffic from the ER to the Golgi via COPII-coated transport vesicles. The five core COPII proteins (Sar1p, Sec23/24p, and Sec13/31p) act in concert to capture cargo proteins and sculpt the ER membrane into vesicles of defined geometry. The molecular details of how the coat proteins deform the lipid bilayer into vesicles are not known. Here we show that the small GTPase Sar1p ...

متن کامل

COPII-mediated protein sorting and concentration in transport vesicles

In eukaryotic cells, intracellular protein transport between the organelles of the secretory pathway is mediated by 50– 80 nm vesicular carriers that are released from a donor organelle and fuse with an appropriate acceptor organelle. The starting point of the secretory route is the endoplasmic reticulum (ER). Once correctly folded and assembled properly in the ER, secretory cargo proteins can ...

متن کامل

Erv14p directs a transmembrane secretory protein into COPII-coated transport vesicles.

Erv14p is a conserved integral membrane protein that traffics in COPII-coated vesicles and localizes to the early secretory pathway in yeast. Deletion of ERV14 causes a defect in polarized growth because Axl2p, a transmembrane secretory protein, accumulates in the endoplasmic reticulum and is not delivered to its site of function on the cell surface. Herein, we show that Erv14p is required for ...

متن کامل

Distinct stages in the recognition, sorting, and packaging of proTGFα into COPII-coated transport vesicles

In addition to its role in forming vesicles from the endoplasmic reticulum (ER), the coat protein complex II (COPII) is also responsible for selecting specific cargo proteins to be packaged into COPII transport vesicles. Comparison of COPII vesicle formation in mammalian systems and in yeast suggested that the former uses more elaborate mechanisms for cargo recognition, presumably to cope with ...

متن کامل

Signals for COPII-dependent export from the ER: what's the ticket out?

Export of many secretory proteins from the endoplasmic reticulum (ER) relies on signal-mediated sorting into ER-derived transport vesicles. Recent work on the coat protein complex II (COPII) provides new insight into the mechanisms and signals that govern this selective export process. Conserved di-acidic and di-hydrophobic motifs found in specific transmembrane cargo proteins are required for ...

متن کامل

ذخیره در منابع من


  با ذخیره ی این منبع در منابع من، دسترسی به آن را برای استفاده های بعدی آسان تر کنید

متن کامل
عنوان ژورنال:
  • Current opinion in cell biology

دوره 9 4  شماره 

صفحات  -

تاریخ انتشار 1997