Ubiquitin ligases in malignant lymphoma.

Abstract:

:The highly controlled degradation of proteins via the ubiquitin-proteasome pathway represents a key mechanism for cell regulation and homeostasis. Ubiquitin-dependent proteolysis, carried out in large part by the E3 ubiquitin ligases, is a critical mode of post-translational modification that is important in regulation of cell cycle progression, signal transduction, gene transcription, antigen receptor signaling, immune response and cell differentiation. Recent studies demonstrate that increasing numbers of proteins with ubiquitin ligase activity are being characterized. Identification and characterization of their substrates indicate that they regulate the turnover of key cell cycle proteins (p27Kip1, p21Cip1, p57Kip2, cyclin E), tumor suppressor proteins (p53, RB), signaling kinases (Src, Zap70, PI-3 kinase), apoptosis regulators (Bcl-2, Bax, Bik) and transcription factors (Myc, NF-kappaB, E1F1), all of which have been implicated in the pathogenesis of malignant lymphoma. Studies to determine the functional role of ubiquitin ligases in the pathogenesis of malignant lymphoma represent potential areas of investigation.

journal_name

Leuk Lymphoma

journal_title

Leukemia & lymphoma

authors

Lim MS,Elenitoba-Johnson KS

doi

10.1080/10428190410001663635

keywords:

subject

Has Abstract

pub_date

2004-07-01 00:00:00

pages

1329-39

issue

7

eissn

1042-8194

issn

1029-2403

journal_volume

45

pub_type

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