ALG-2 directly binds Sec31A and localizes at endoplasmic reticulum exit sites in a Ca2+-dependent manner
- 22 December 2006
- journal article
- Published by Elsevier in Biochemical and Biophysical Research Communications
- Vol. 353 (3) , 756-763
- https://doi.org/10.1016/j.bbrc.2006.12.101
Abstract
No abstract availableKeywords
This publication has 20 references indexed in Scilit:
- The multiple personalities of AlixJournal of Cell Science, 2006
- Endosomal and non-endosomal functions of ESCRT proteinsTrends in Cell Biology, 2006
- Do Alix and ALG‐2 really control endosomes for better or for worse?Biology of the Cell, 2006
- The penta-EF-hand protein ALG-2 interacts directly with the ESCRT-I component TSG101, and Ca2+-dependently co-localizes to aberrant endosomes with dominant-negative AAA ATPase SKD1/Vps4BBiochemical Journal, 2005
- p125 Is Localized in Endoplasmic Reticulum Exit Sites and Involved in Their OrganizationJournal of Biological Chemistry, 2005
- The Penta-EF-Hand Protein ALG-2 Interacts with a Region Containing PxY Repeats in Alix/AIP1, Which Is Required for the Subcellular Punctate Distribution of the Amino-Terminal Truncation Form of Alix/AIP1The Journal of Biochemistry, 2004
- Properties of the co‐chaperone protein p23 erroneously attributed to ALG‐2 (apoptosis‐linked gene 2)FEBS Letters, 2003
- The ALG-2-interacting Protein Alix Associates with CHMP4b, a Human Homologue of Yeast Snf7 That Is Involved in Multivesicular Body SortingJournal of Biological Chemistry, 2003
- Up-Regulation of ALG-2 in Hepatomas and Lung Cancer TissueThe American Journal of Pathology, 2003
- Structures, functions and molecular evolution of the penta-EF-hand Ca2+-binding proteinsBiochimica et Biophysica Acta (BBA) - Proteins and Proteomics, 2002