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Structure of Gq-p63RhoGEF-RhoA Complex Reveals a Pathway for the Activation of RhoA by GPCRs
Oleh:
Lutz, Susanne
;
Shankaranarayanan, Aruna
;
Coco, Cassandra
;
Ridilla, Marc
;
Nance, Mark R.
;
Vettel, Christiane
;
Baltus, Doris
;
Evelyn, Chris R.
;
Neubig, Richard R.
;
Wieland, Thomas
;
Tesmer, John J.G.
Jenis:
Article from Bulletin/Magazine
Dalam koleksi:
SCIENCE (keterangan: ada di Proquest) vol. 318 no. 5858 (Dec. 2007)
,
page 1923.
Ketersediaan
Perpustakaan FK
Nomor Panggil:
S01.K.2007.09
Non-tandon:
1 (dapat dipinjam: 0)
Tandon:
tidak ada
Lihat Detail Induk
Isi artikel
The guanine nucleotide exchange factor p63RhoGEF is an effector of the heterotrimeric guanine nucleotide–binding protein (G protein) Gq and thereby links Gq-coupled receptors (GPCRs) to the activation of the small-molecular-weight G protein RhoA. We determined the crystal structure of the Gq-p63RhoGEF-RhoA complex, detailing the interactions of Gq with the Dbl and pleckstrin homology (DH and PH) domains of p63RhoGEF. These interactions involve the effector-binding site and the C-terminal region of Gq and appear to relieve autoinhibition of the catalytic DH domain by the PH domain. Trio, Duet, and p63RhoGEF are shown to constitute a family of Gq effectors that appear to activate RhoA both in vitro and in intact cells. We propose that this structure represents the crux of an ancient signal transduction pathway that is expected to be important in an array of physiological processes.
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