Receptor-C-k regulated membrane-bound 125 kDa protein having affinity for genomic sterol regulatory sequence

Authors
Citation
D. Kaul et M. Kaur, Receptor-C-k regulated membrane-bound 125 kDa protein having affinity for genomic sterol regulatory sequence, MOL C BIOCH, 216(1-2), 2001, pp. 141-143
Citations number
14
Categorie Soggetti
Cell & Developmental Biology
Journal title
MOLECULAR AND CELLULAR BIOCHEMISTRY
ISSN journal
03008177 → ACNP
Volume
216
Issue
1-2
Year of publication
2001
Pages
141 - 143
Database
ISI
SICI code
0300-8177(200101)216:1-2<141:RRM1KP>2.0.ZU;2-N
Abstract
The study addressed, to resolve the role of Receptor-C-k activation in the proteolytic maturation of 125 kDa (membrane bound) sterol regulatory elemen t binding protein (SREBP), revealed that Receptor-C-k dependent signalling is not only responsible for the proteoloytic cleavage of this 125 kDa SREBP resulting in the generation of an active 47 kDa factor but also Receptor-C -k protein has high binding affinity for both 125 kDa SREBP as well as its cleaved 47 kDa product. Based upon these coupled with our earlier findings, we propose that Receptor-C-k may be regulating genes, have sterol regulato ry element (SRE) in their promoter region, through the proteolytic maturati on of 125 kDa SREBP into an active 47 kDa transcription factor.