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Pex14p, more than just a docking protein.
- Source :
-
Biochimica et biophysica acta [Biochim Biophys Acta] 2006 Dec; Vol. 1763 (12), pp. 1574-84. Date of Electronic Publication: 2006 Sep 14. - Publication Year :
- 2006
-
Abstract
- After binding newly synthesized peroxisomal matrix proteins in the cytosol, the second task of Pex5p, the peroxisomal cycling receptor, is to carry these proteins to the peroxisomal membrane. Defining the nature of the events that occur at this membrane system and which ultimately result in the translocation of the cargo proteins into the matrix of the organelle and in the recycling of Pex5p back to the cytosol, is one of the major goals of the research in this field. Presently, it is generally accepted that all these steps are promoted by a large protein complex embedded in the peroxisomal membrane. This docking/translocation machinery or importomer, as it is often called, comprises many different peroxins of which one of the best characterized is Pex14p. Here, we review data regarding this membrane peroxin with emphasis on the interactions that it establishes with Pex5p. The available evidence suggests that the key to understand how folded proteins are capable of passing an apparently impermeable membrane may largely reside in this pair of peroxins.
- Subjects :
- Animals
Humans
Intracellular Membranes metabolism
Membrane Transport Proteins
Peroxins
Peroxisome-Targeting Signal 1 Receptor
Protein Binding
Protein Interaction Mapping
Protein Transport
Receptors, Cytoplasmic and Nuclear physiology
Saccharomyces cerevisiae Proteins physiology
Membrane Proteins physiology
Peroxisomes metabolism
Protein Folding
Repressor Proteins physiology
Subjects
Details
- Language :
- English
- ISSN :
- 0006-3002
- Volume :
- 1763
- Issue :
- 12
- Database :
- MEDLINE
- Journal :
- Biochimica et biophysica acta
- Publication Type :
- Academic Journal
- Accession number :
- 17046076
- Full Text :
- https://doi.org/10.1016/j.bbamcr.2006.09.002