Positioning proteasomes

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3 Proteasomes

The major enzyme system catalysing the degradation of intracellular proteins is the proteasome system. A central inner chamber of the cylinder-shaped 20 S proteasome contains the active site, formed by N-terminal threonine residues. The 20 S proteasomes are extremely inefficient in degrading folded protein substrates and therefore one or two multisubunit 19 S regulatory particles bind to one or...

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Proteasomes: multicatalytic proteinase complexes.

The multicatalytic proteinase complex (proteasome) is a highmolecular-mass (approximately 700 kDa) intracellular proteinase which has been isolated under a variety of different names from a wide variety of eukaryotic cells and tissues (reviewed, Rivett, 1989a; Orlowski, 1990). The proteinase complex is composed of at least 24 subunits which include many different polypeptides arranged in a cyli...

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Intracellular localization of proteasomes.

Proteasomes are present in the cytoplasm and in the nuclei of all eukaryotic cells, however their relative abundance within those compartments is highly variable. In the cytoplasm, proteasomes associate with the centrosomes, cytoskeletal networks and the outer surface of the endoplasmic reticulum (ER). In the nucleus, proteasomes are present throughout the nucleoplasm but are void from the nucl...

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Nuclear Import of Yeast Proteasomes

Proteasomes are highly conserved protease complexes responsible for the degradation of aberrant and short-lived proteins. In highly proliferating yeast and mammalian cells, proteasomes are predominantly nuclear. During quiescence and cell cycle arrest, proteasomes accumulate in granules in close proximity to the nuclear envelope/ER. With prolonged quiescence in yeast, these proteasome granules ...

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Proteasomes: Machines for All Reasons

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ژورنال

عنوان ژورنال: Journal of Cell Biology

سال: 2006

ISSN: 1540-8140,0021-9525

DOI: 10.1083/jcb.1743rr1