Endocytosis of receptor tyrosine kinases

LK Goh, A Sorkin - Cold Spring Harbor perspectives in …, 2013 - cshperspectives.cshlp.org
Endocytosis is the major regulator of signaling from receptor tyrosine kinases (RTKs). The
canonical model of RTK endocytosis involves rapid internalization of an RTK activated by …

[HTML][HTML] Molecular mechanisms underlying endocytosis and sorting of ErbB receptor tyrosine kinases

H Waterman, Y Yarden - FEBS letters, 2001 - Elsevier
The major process that regulates the amplitude and kinetics of signal transduction by
tyrosine kinase receptors is endocytic removal of active ligand–receptor complexes from the …

The juxtamembrane region of the EGF receptor functions as an activation domain

MR Brewer, SH Choi, D Alvarado, K Moravcevic… - Molecular cell, 2009 - cell.com
In several growth factor receptors, the intracellular juxtamembrane (JM) region participates
in autoinhibitory interactions that must be disrupted for tyrosine kinase activation. Using …

Physical interaction between epidermal growth factor receptor and DNA-dependent protein kinase in mammalian cells

D Bandyopadhyay, M Mandal, L Adam… - Journal of Biological …, 1998 - ASBMB
Binding of extracellular ligands to epidermal growth factor receptors (EGFR) activate signal
transduction pathways associated with cell proliferation, and these events are inhibited by …

The human epidermal growth factor receptor contains a juxtamembrane calmodulin-binding site

J Martín-Nieto, A Villalobo - Biochemistry, 1998 - ACS Publications
A ligand-insensitive form of the human epidermal growth factor receptor (EGFR) was
enriched by Ca2+-dependent calmodulin-affinity chromatography purification. The basic …

Calmodulin‐mediated regulation of the epidermal growth factor receptor

P Sánchez‐González, K Jellali, A Villalobo - The FEBS journal, 2010 - Wiley Online Library
In this review, we first describe the mechanisms by which the epidermal growth factor
receptor generates a Ca2+ signal and, subsequently, we compile the available experimental …

Tyrosine phosphorylation of the β2 subunit of clathrin adaptor complex AP-2 reveals the role of a di-leucine motif in the epidermal growth factor receptor trafficking

F Huang, X Jiang, A Sorkin - Journal of Biological Chemistry, 2003 - ASBMB
Tyrosine phosphorylation of the β2 subunit of clathrin adaptor complex AP-2 was detected in
three types of cells treated with epidermal growth factor (EGF). The tyrosine phosphorylation …

Identification of a di-leucine motif within the C terminus domain of the Menkes disease protein that mediates endocytosis from the plasma membrane

MJ Francis, EE Jones, ER Levy… - Journal of cell …, 1999 - journals.biologists.com
The protein encoded by the Menkes disease gene (MNK) is localised to the Golgi apparatus
and cycles between the trans-Golgi network and the plasma membrane in cultured cells on …

Interactions between the juxtamembrane domain of the EGFR and calmodulin measured by surface plasmon resonance

S Aifa, K Johansen, UK Nilsson, B Liedberg… - Cellular signalling, 2002 - Elsevier
One early response to epidermal growth factor receptor (EGFR) activation is an increase in
intracellular calcium. We have used surface plasmon resonance (SPR) to study real-time …

Proteasome-mediated proteolysis of the interleukin-10 receptor is important for signal downregulation

SHY Wei, A Ming-Lum, Y Liu, D Wallach… - Journal of interferon & …, 2006 - liebertpub.com
The cytokine interleukin-10 (IL-10) is an important regulator of immune cell function,
proliferation, and survival. The IL-10 receptor (IL-10R) consists of two subunits, IL-10R1 and …