p125 Is Localized in Endoplasmic Reticulum Exit Sites and Involved in Their Organization
Open Access
- 1 March 2005
- journal article
- Published by Elsevier in Journal of Biological Chemistry
- Vol. 280 (11) , 10141-10148
- https://doi.org/10.1074/jbc.m409673200
Abstract
No abstract availableKeywords
This publication has 47 references indexed in Scilit:
- Global analysis of protein localization in budding yeastNature, 2003
- Multiple Cargo Binding Sites on the COPII Subunit Sec24p Ensure Capture of Diverse Membrane Proteins into Transport VesiclesCell, 2003
- SNARE Selectivity of the COPII CoatCell, 2003
- SVIP Is a Novel VCP/p97-interacting Protein Whose Expression Causes Cell VacuolationMolecular Biology of the Cell, 2003
- Cargo selection into COPII vesicles is driven by the Sec24p subunitThe EMBO Journal, 2002
- Maintenance of Golgi structure and function depends on the integrity of ER exportThe Journal of cell biology, 2001
- Determination of Functional Regions of p125, a Novel Mammalian Sec23p-Interacting ProteinBiochemical and Biophysical Research Communications, 2000
- Kinase Signaling Initiates Coat Complex II (COPII) Recruitment and Export from the Mammalian Endoplasmic ReticulumJournal of Biological Chemistry, 2000
- Vesicular Tubular Clusters between the ER and Golgi Mediate Concentration of Soluble Secretory Proteins by Exclusion from COPI-Coated VesiclesPublished by Elsevier ,1999
- Identification, by a monoclonal antibody, of a 53-kD protein associated with a tubulo-vesicular compartment at the cis-side of the Golgi apparatus.The Journal of cell biology, 1988