Transferring substrates to the 26S proteasome.

Rasmus Hartmann-Petersen; Michael Seeger; Colin Gordon

doi:10.1016/S0968-0004(02)00002-6

Transferring substrates to the 26S proteasome.

Rasmus Hartmann-Petersen, Michael Seeger, Colin Gordon

Biomolecular Sciences

137 Citations (Scopus)

Abstract

Ubiquitin-dependent protein degradation is not only involved in the recycling of amino acids from damaged or misfolded proteins but also represents an essential and deftly controlled mechanism for modulating the levels of key regulatory proteins. Chains of ubiquitin conjugated to a substrate protein specifically target it for degradation by the 26S proteasome, a huge multi-subunit protein complex found in all eukaryotic cells. Recent reports have clarified some of the molecular mechanisms involved in the transfer of ubiquitinated substrates from the ubiquitination machinery to the proteasome. This novel substrate transportation step in the ubiquitin-proteasome pathway seems to occur either directly or indirectly via certain substrate-recruiting proteins and appears to involve chaperones.

Original language	English
Journal	TIBS -Trends in Biochemical Sciences. Regular ed.
Volume	28
Issue number	1
Pages (from-to)	26-31
Number of pages	5
ISSN	0968-0004
DOIs	https://doi.org/10.1016/S0968-0004(02)00002-6
Publication status	Published - 2003

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10.1016/S0968-0004(02)00002-6

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title = "Transferring substrates to the 26S proteasome.",

abstract = "Ubiquitin-dependent protein degradation is not only involved in the recycling of amino acids from damaged or misfolded proteins but also represents an essential and deftly controlled mechanism for modulating the levels of key regulatory proteins. Chains of ubiquitin conjugated to a substrate protein specifically target it for degradation by the 26S proteasome, a huge multi-subunit protein complex found in all eukaryotic cells. Recent reports have clarified some of the molecular mechanisms involved in the transfer of ubiquitinated substrates from the ubiquitination machinery to the proteasome. This novel substrate transportation step in the ubiquitin-proteasome pathway seems to occur either directly or indirectly via certain substrate-recruiting proteins and appears to involve chaperones.",

author = "Rasmus Hartmann-Petersen and Michael Seeger and Colin Gordon",

note = "Keywords: Cysteine Endopeptidases; Molecular Chaperones; Multienzyme Complexes; Proteasome Endopeptidase Complex; Substrate Specificity; Ubiquitin",

year = "2003",

doi = "10.1016/S0968-0004(02)00002-6",

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journal = "Trends in Biochemical Sciences",

issn = "0968-0004",

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T1 - Transferring substrates to the 26S proteasome.

AU - Hartmann-Petersen, Rasmus

AU - Seeger, Michael

AU - Gordon, Colin

N1 - Keywords: Cysteine Endopeptidases; Molecular Chaperones; Multienzyme Complexes; Proteasome Endopeptidase Complex; Substrate Specificity; Ubiquitin

PY - 2003

Y1 - 2003

N2 - Ubiquitin-dependent protein degradation is not only involved in the recycling of amino acids from damaged or misfolded proteins but also represents an essential and deftly controlled mechanism for modulating the levels of key regulatory proteins. Chains of ubiquitin conjugated to a substrate protein specifically target it for degradation by the 26S proteasome, a huge multi-subunit protein complex found in all eukaryotic cells. Recent reports have clarified some of the molecular mechanisms involved in the transfer of ubiquitinated substrates from the ubiquitination machinery to the proteasome. This novel substrate transportation step in the ubiquitin-proteasome pathway seems to occur either directly or indirectly via certain substrate-recruiting proteins and appears to involve chaperones.

AB - Ubiquitin-dependent protein degradation is not only involved in the recycling of amino acids from damaged or misfolded proteins but also represents an essential and deftly controlled mechanism for modulating the levels of key regulatory proteins. Chains of ubiquitin conjugated to a substrate protein specifically target it for degradation by the 26S proteasome, a huge multi-subunit protein complex found in all eukaryotic cells. Recent reports have clarified some of the molecular mechanisms involved in the transfer of ubiquitinated substrates from the ubiquitination machinery to the proteasome. This novel substrate transportation step in the ubiquitin-proteasome pathway seems to occur either directly or indirectly via certain substrate-recruiting proteins and appears to involve chaperones.

U2 - 10.1016/S0968-0004(02)00002-6

DO - 10.1016/S0968-0004(02)00002-6

M3 - Journal article

C2 - 12517449

SN - 0968-0004

VL - 28

SP - 26

EP - 31

JO - Trends in Biochemical Sciences

JF - Trends in Biochemical Sciences

IS - 1

ER -

Transferring substrates to the 26S proteasome.

Abstract

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