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Human pex19p binds peroxisomal integral membrane proteins at regions distinct from their sorting sequences.
- Source :
-
Molecular and cellular biology [Mol Cell Biol] 2001 Jul; Vol. 21 (13), pp. 4413-24. - Publication Year :
- 2001
-
Abstract
- The molecular machinery underlying peroxisomal membrane biogenesis is not well understood. The observation that cells deficient in the peroxins Pex3p, Pex16p, and Pex19p lack peroxisomal membrane structures suggests that these molecules are involved in the initial stages of peroxisomal membrane formation. Pex19p, a predominantly cytosolic protein that can be farnesylated, binds multiple peroxisomal integral membrane proteins, and it has been suggested that it functions as a soluble receptor for the targeting of peroxisomal membrane proteins (PMPs) to the peroxisome. An alternative view proposes that Pex19p functions as a chaperone at the peroxisomal membrane. Here, we show that the peroxisomal sorting determinants and the Pex19p-binding domains of a number of PMPs are distinct entities. In addition, we extend the list of peroxins with which human Pex19p interacts to include the PMP Pex16p and show that Pex19p's CaaX prenylation motif is an important determinant in the affinity of Pex19p for Pex10p, Pex11pbeta, Pex12p, and Pex13p.
- Subjects :
- Amino Acid Sequence
Animals
Binding Sites
CHO Cells
Cell Fractionation
Cricetinae
Genes, Reporter genetics
Humans
Membrane Proteins genetics
Microscopy, Fluorescence
Molecular Sequence Data
Peroxisomes chemistry
Plasmids genetics
Plasmids metabolism
Protein Binding
Protein Conformation
Recombinant Fusion Proteins genetics
Recombinant Fusion Proteins metabolism
Transfection
Two-Hybrid System Techniques
Fungal Proteins metabolism
Membrane Proteins metabolism
Peroxisomes metabolism
Protein Sorting Signals
Subjects
Details
- Language :
- English
- ISSN :
- 0270-7306
- Volume :
- 21
- Issue :
- 13
- Database :
- MEDLINE
- Journal :
- Molecular and cellular biology
- Publication Type :
- Academic Journal
- Accession number :
- 11390669
- Full Text :
- https://doi.org/10.1128/MCB.21.13.4413-4424.2001