In:
Science, American Association for the Advancement of Science (AAAS), Vol. 341, No. 6143 ( 2013-07-19), p. 242-243
Abstract:
Protein synthesis is elevated in many cancers ( 1 ). To cope with increased protein load and protein folding defects caused by genetic abnormalities, malignant cells bolster their chaperone system. Heat-shock transcription factor 1 (HSF1) is a major activator of chaperone-encoding genes. In cancer cells, HSF1 also affects the transcription of genes that are implicated in tumorigenesis ( 2 ), thereby shaping the “malignant transcriptome.” On page 250 of this issue, Santagata et al. ( 3 ) suggest that HSF1 acts as a central node of a regulatory network that “senses” messenger RNA (mRNA) translation rates and enables malignant cells to respond to increased protein loads by reprogramming transcription.
Type of Medium:
Online Resource
ISSN:
0036-8075
,
1095-9203
DOI:
10.1126/science.1242359
Language:
English
Publisher:
American Association for the Advancement of Science (AAAS)
Publication Date:
2013
detail.hit.zdb_id:
128410-1
detail.hit.zdb_id:
2066996-3
detail.hit.zdb_id:
2060783-0
SSG:
11
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