Receptor tyrosine kinase ubiquitylation involves the dynamic regulation of Cbl-Spry2 by intersectin 1 and the Shp2 tyrosine phosphatase

MN Okur, A Russo, JP O'Bryan - Molecular and cellular biology, 2014 - Taylor & Francis
Ubiquitylation of receptor tyrosine kinases (RTKs) regulates their trafficking and lysosomal
degradation. The multidomain scaffolding protein intersectin 1 (ITSN1) is an important …

Intersectin 1 enhances Cbl ubiquitylation of epidermal growth factor receptor through regulation of Sprouty2-Cbl interaction

MN Okur, J Ooi, CW Fong, N Martinez… - … and cellular biology, 2012 - Taylor & Francis
Ubiquitylation of receptor tyrosine kinases plays a critical role in regulating the trafficking
and lysosomal degradation of these important signaling molecules. We identified the …

Sprouty2 acts at the Cbl/CIN85 interface to inhibit epidermal growth factor receptor downregulation

K Haglund, MHH Schmidt, ESM Wong, GR Guy… - EMBO …, 2005 - embopress.org
The ubiquitin ligase Cbl mediates ubiquitination of activated receptor tyrosine kinases
(RTKs) and interacts with endocytic scaffold complexes, including CIN85/endophilins, to …

Intersectin regulates epidermal growth factor receptor endocytosis, ubiquitylation, and signaling

NP Martin, RP Mohney, S Dunn, M Das, E Scappini… - Molecular …, 2006 - ASPET
Receptor tyrosine kinases (RTKs) are critical for normal cell growth, differentiation, and
development, but they contribute to various pathological conditions when disrupted …

[HTML][HTML] Tesk1 interacts with Spry2 to abrogate its inhibition of ERK phosphorylation downstream of receptor tyrosine kinase signaling

S Chandramouli, CY Yu, P Yusoff, DH Lao… - Journal of Biological …, 2008 - ASBMB
The Sprouty (Spry) proteins function as inhibitors of the Ras-ERK pathway downstream of
various receptor tyrosine kinases. In this study, we have identified Tesk1 (testicular protein …

[HTML][HTML] Sprouty2 attenuates epidermal growth factor receptor ubiquitylation and endocytosis, and consequently enhances Ras/ERK signalling

ESM Wong, CW Fong, J Lim, P Yusoff, BC Low… - The EMBO …, 2002 - embopress.org
Drosophila Sprouty (dSpry) was genetically identified as a novel antagonist of fibroblast
growth factor receptor (FGFR), epidermal growth factor receptor (EGFR) and Sevenless …

[HTML][HTML] Sprouty2 interacts with protein kinase Cδ and disrupts phosphorylation of protein kinase D1

SY Chow, CY Yu, GR Guy - Journal of biological chemistry, 2009 - ASBMB
The Sprouty (Spry) proteins act as inhibitors of the Ras/ERK pathway downstream of
receptor tyrosine kinases. In this study, we report a novel interaction between protein kinase …

CrkL is a novel target of Sprouty2 in fibroblast growth factor signaling

T Satoh, S Torii, K Nakayama, E Nishida - Genes to cells, 2010 - Wiley Online Library
Sprouty, an inhibitor of receptor tyrosine kinase signaling, plays an important role in the
regulation of a wide variety of biological processes. Although it is established that the …

[HTML][HTML] HECT domain-containing E3 ubiquitin ligase Nedd4 interacts with and ubiquitinates Sprouty2

F Edwin, K Anderson, TB Patel - Journal of biological chemistry, 2010 - ASBMB
Sprouty (Spry) proteins are important regulators of receptor tyrosine kinase signaling in
development and disease. Alterations in cellular Spry content have been associated with …

Regulation of colony-stimulating factor 1 receptor signaling by the SH2 domain-containing tyrosine phosphatase SHPTP1

HE Chen, S Chang, T Trub, BG Neel - Molecular and cellular …, 1996 - Am Soc Microbiol
Abstract SHPTP1 (PTP1C, HCP, SHP) is an SH2 domain-containing tyrosine phosphatase
expressed predominantly in hematopoietic cells. A frameshift mutation in the SHPTP1 gene …