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Parkin interacts with the proteasome subunit α4
Author(s) -
Dächsel J.C.,
Lücking C.B.,
Deeg S.,
Schultz E.,
Lalowski M.,
Casademunt E.,
Corti O.,
Hampe C.,
Patenge N.,
Vaupel K.,
Yamamoto A.,
Dichgans M.,
Brice A.,
Wanker E.E.,
Kahle P.J.,
Gasser T.
Publication year - 2005
Publication title -
febs letters
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 1.593
H-Index - 257
eISSN - 1873-3468
pISSN - 0014-5793
DOI - 10.1016/j.febslet.2005.06.003
Subject(s) - parkin , ubiquitin , ubiquitin ligase , proteasome , protein subunit , hek 293 cells , neurodegeneration , microbiology and biotechnology , biology , genetics , chemistry , parkinson's disease , gene , disease , medicine , pathology
Mutations in the parkin gene encoding an E3 ligase are responsible for autosomal recessive Parkinson's disease. Putative parkin substrates and interacting partners have been identified, but the molecular mechanism underlying parkin‐related neurodegeneration is still unclear. We have identified the 20S proteasomal subunit α4 (synonyms: PSMA7, XAPC7, subunit alpha type 7) as a new interacting partner of parkin. The C‐terminal IBR‐RING domain of parkin and the C‐terminal part of α4 were essential for the interaction. Biochemical studies revealed that α4 was not a substrate for parkin‐dependent ubiquitylation. Putative functions of the interaction might therefore be substrate presentation to the proteasome or regulation of proteasomal activity. Full‐length parkin and parkin lacking the N‐terminal ubiquitin‐like domain slightly increased the proteasomal activity in HEK 293T cells, in line with the latter hypothesis.