The fates of proteins in cells.
Nascent polypeptide chains are in a dangerous situation as soon as they leave their place of birth, the channel of the large ribosomal subunit: more than 20 different pathways for the degradation of proteins exist in cells. Chaperones protect and guide the young protein molecules and support their correct foldings. Targeting signals direct the proteins to the organelles of their destination. The lysosome is the site of random degradation, while the proteasome is highly selective. Although these two organelles provide the most important pathways for the degradation of long- and short-lived proteins, other pathways with roles in deciding the fate of cellular proteins must also be considered.
Bohley
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Physiologisch-Chemisches Institut der Universität, Tübingen.
D000595:Amino Acid Sequence; D000818:Animals; D002403:Cathepsins / Q000378:metabolism; D002467:Cell Nucleus / Q000378:metabolism; D002477:Cells / Q000378:metabolism* / Q000648:ultrastructure; D018833:Chaperonins / Q000502:physiology*; D003600:Cytosol / Q000378:metabolism; D004721:Endoplasmic Reticulum / Q000378:metabolism; D006801:Humans; D008961:Models, Structural; D008969:Molecular Sequence Data; D015388:Organelles / Q000378:metabolism*; D014176:Protein Biosynthesis; D017510:Protein Folding; D021382:Protein Sorting Signals / Q000737:chemistry / Q000378:metabolism; D011506:Proteins / Q000737:chemistry / Q000378:metabolism*
D021382:Protein Sorting Signals; D011506:Proteins; D002403:Cathepsins; D018833:Chaperonins