PEX19 is a predominantly cytosolic chaperone and import receptor for class 1 peroxisomal membrane proteins
| Autor: | Stephen Jay Gould, Jacob M. Jones, James C. Morrell |
|---|---|
| Jazyk: | angličtina |
| Rok vydání: | 2004 |
| Předmět: |
Signal peptide
peroxisome protein import posttranslational Zellweger syndrome PEX3 Peroxin Plasma protein binding Article Cell Line Cytosol Peroxisomes Humans biology Membrane transport protein Membrane Proteins Membrane Transport Proteins Cell Biology Intracellular Membranes Cell biology Transport protein Protein Structure Tertiary Protein Transport Biochemistry Membrane protein Cytoplasm Chaperone (protein) biology.protein RNA Interference Molecular Chaperones Protein Binding Signal Transduction |
| Zdroj: | The Journal of Cell Biology |
| ISSN: | 1540-8140 0021-9525 |
| Popis: | Integral peroxisomal membrane proteins (PMPs) are synthesized in the cytoplasm and imported posttranslationally. Here, we demonstrate that PEX19 binds and stabilizes newly synthesized PMPs in the cytosol, binds to multiple PMP targeting signals (mPTSs), interacts with the hydrophobic domains of PMP targeting signals, and is essential for PMP targeting and import. These results show that PEX19 functions as both a chaperone and an import receptor for newly synthesized PMPs. We also demonstrate the existence of two PMP import mechanisms and two classes of mPTSs: class 1 mPTSs, which are bound by PEX19 and imported in a PEX19-dependent manner, and class 2 mPTSs, which are not bound by PEX19 and mediate protein import independently of PEX19. |
| Databáze: | OpenAIRE |
| Externí odkaz: |
|