Protein translocation machineries: how organelles bring in matrix proteins.
Eukaryotic cells contain several thousands of proteins that have to be accurately partitioned over the components of the cytoplasm (cytosol or any of the known organelles) to allow proper cell function. To this end, various specific topogenic signals have been designed as well as highly selective protein translocation machineries that ensure that each newly synthesized polypeptide reaches its correct subcellular destination or, in case of secretory proteins, is exported to the cell exterior. This contribution gives an overview regarding the principles of the main examples of polypeptide sorting and translocation, with emphasis on the function of cofactor binding in peroxisomal matrix protein import.
Gunkel
Katja
K
Eukaryotic Microbiology, Groningen Biomolecular Sciences and Biotechnology Institute (GBB), University of Groningen, P.O. Box 14, 9750 AA Haren, The Netherlands.
Veenhuis
Marten
M
van der Klei
Ida J
IJ
D005057:Eukaryotic Cells / Q000378:metabolism; D016326:Extracellular Matrix Proteins / Q000378:metabolism*; D015388:Organelles / Q000378:metabolism*; D020675:Peroxisomes / Q000737:chemistry / Q000378:metabolism*; D021382:Protein Sorting Signals / Q000235:genetics; D021381:Protein Transport; D015003:Yeasts
D016326:Extracellular Matrix Proteins; D021382:Protein Sorting Signals