Rabip4' is an effector of rab5 and rab4 and regulates transport through early endosomes
| Autor: | Annemarie van der Heijden, Magda Deneka, Denise van Suylekom, Walther J. van Venrooij, Michael A. Fouraux, Peter van der Sluijs, Ger J. M. Pruijn, Viorica Ivan, Jos Raymackers |
|---|---|
| Rok vydání: | 2004 |
| Předmět: |
GTP'
Endosome media_common.quotation_subject Molecular Sequence Data Vesicular Transport Proteins Endosomes Biology Endocytosis Wortmannin EEA1 Phosphatidylinositol 3-Kinases chemistry.chemical_compound Humans Amino Acid Sequence Enzyme Inhibitors Fluorescent Antibody Technique Indirect Internalization Molecular Biology Cells Cultured Phosphoinositide-3 Kinase Inhibitors rab5 GTP-Binding Proteins media_common rab4 GTP-Binding Proteins Peripheral membrane protein Transferrin Membrane Proteins Bio-Molecular Chemistry Biological Transport Articles Cell Biology Protein Structure Tertiary Cell biology Androstadienes chemistry FYVE domain HeLa Cells |
| Zdroj: | Molecular Biology of the Cell, 15, 611-24 Molecular Biology of the Cell, 15, 2, pp. 611-24 |
| ISSN: | 1059-1524 |
| DOI: | 10.1091/mbc.e03-05-0343 |
| Popis: | Contains fulltext : 57913.pdf (Publisher’s version ) (Open Access) We describe the characterization of an 80-kDa protein cross-reacting with a monoclonal antibody against the human La autoantigen. The 80-kDa protein is a variant of rabip4 with an N-terminal extension of 108 amino acids and is expressed in the same cells. For this reason, we named it rabip4'. rabip4' is a peripheral membrane protein, which colocalized with internalized transferrin and EEA1 on early endosomes. Membrane association required the presence of the FYVE domain and was perturbed by the phosphatidylinositol 3-kinase inhibitor wortmannin. Expression of a dominant negative rabip4' mutant reduced internalization and recycling of transferrin from early endosomes, suggesting that it may be functionally linked to rab4 and rab5. In agreement with this, we found that rabip4' colocalized with the two GTPases on early endosomes and bound specifically and simultaneously to the GTP form of both rab4 and rab5. We conclude that rabip4' may coordinate the activities of rab4 and rab5, regulating membrane dynamics in the early endosomal system. |
| Databáze: | OpenAIRE |
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