G
Gayathri Swaminathan
Researcher at Stanford University
Publications - 19
Citations - 1021
Gayathri Swaminathan is an academic researcher from Stanford University. The author has contributed to research in topics: Signal transduction & Endocytosis. The author has an hindex of 12, co-authored 16 publications receiving 918 citations. Previous affiliations of Gayathri Swaminathan include University of Pennsylvania & Temple University.
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Journal ArticleDOI
The Cbl family proteins: ring leaders in regulation of cell signaling.
TL;DR: This review will endeavor to provide a summary of current studies focused on the effects of Cbl proteins on various biological processes and the mechanism of these effects.
Journal ArticleDOI
Site-specific ubiquitination exposes a linear motif to promote interferon-α receptor endocytosis
K.G. Suresh Kumar,Herve Barriere,Christopher J. Carbone,Jianghuai Liu,Gayathri Swaminathan,Ping Xu,Ying Li,Darren P. Baker,Junmin Peng,Gergely L. Lukacs,Serge Y. Fuchs +10 more
TL;DR: It is revealed that IFNAR1 is polyubiquitinated via both Lys48- and Lys63-linked chains, implicating cooperation between site-specific ubiquitination and the linear endocytic motif in regulating this process.
Journal ArticleDOI
Beyond the RING: CBL proteins as multivalent adapters.
TL;DR: Experimental evidence for these functions, interrelations between them, and their biological significance are addressed in this review, with the main accent placed on the adapter functions of Cbl proteins.
Journal ArticleDOI
Polyubiquitination of prolactin receptor stimulates its internalization, postinternalization sorting, and degradation via the lysosomal pathway.
Bentley Varghese,Herve Barriere,Christopher J. Carbone,Anamika Banerjee,Gayathri Swaminathan,Alexander Plotnikov,Ping Xu,Junmin Peng,Vincent Goffin,Gergely L. Lukacs,Serge Y. Fuchs +10 more
TL;DR: Evidence is provided that PRLr is internalized and primarily degraded via the lysosomal pathway, and how specific ubiquitination may regulate early and late stages of endocytosis ofPRLr and of related receptors to contribute to the negative regulation of the magnitude and duration of downstream signaling is discussed.
Journal ArticleDOI
TULA: an SH3- and UBA-containing protein that binds to c-Cbl and ubiquitin
Elena A Feshchenko,Evgeniya V. Smirnova,Gayathri Swaminathan,Anjali M Teckchandani,Rachana Agrawal,Hamid Band,Hamid Band,Xiaolong Zhang,Xiaolong Zhang,Roland S. Annan,Steven A. Carr,Steven A. Carr,Alexander Y. Tsygankov +12 more
TL;DR: The study indicates that TULA counters the inhibitory effect of c-Cbl on protein tyrosine kinases and, thus, may be involved in the regulation of biological effects of c.Cbl.