The importance of being proline: the interaction of proline‐rich motifs in signaling proteins with their cognate domains

BK Kay, MP Williamson, M Sudol - The FASEB journal, 2000 - Wiley Online Library
ABSTRACT A common focus among molecular and cellular biologists is the identification of
proteins that interact with each other. Yeast two‐hybrid, cDNA expression library screening …

Met receptor tyrosine kinase: enhanced signaling through adapter proteins

KA Furge, YW Zhang, GF Vande Woude - Oncogene, 2000 - nature.com
The Met receptor tyrosine kinase is the prototypic member of a small subfamily of growth
factor receptors that when activated induce mitogenic, motogenic, and morphogenic cellular …

The WW domain of Yes-associated protein binds a proline-rich ligand that differs from the consensus established for Src homology 3-binding modules.

HI Chen, M Sudol - Proceedings of the National Academy of …, 1995 - National Acad Sciences
The WW domain has previously been described as a motif of 38 semiconserved residues
found in seemingly unrelated proteins, such as dystrophin, Yes-associated protein (YAP) …

Crk family adaptors–signalling complex formation and biological roles

SM Feller - Oncogene, 2001 - nature.com
Crk family adaptors are widely expressed and mediate the timely formation of signal
transduction protein complexes upon a variety of extracellular stimuli, including various …

Modular peptide recognition domains in eukaryotic signaling

J Kuriyan, D Cowburn - Annual review of biophysics and …, 1997 - annualreviews.org
▪ Abstract A characteristic feature of cellular signal transduction pathways in eukaryotes is
the separation of catalysis from target recognition. Several modular domains that recognize …

Regulation of Btk function by a major autophosphorylation site within the SH3 domain

H Park, MI Wahl, DEH Afar, CW Turck, DJ Rawlings… - Immunity, 1996 - cell.com
Bruton's tyrosine kinase (Btk) plays a crucial role in B cell development. Overexpression of
Btk with a Src family kinase increases tyrosine phosphorylation and catalytic activity of Btk …

[HTML][HTML] Crystal structure of the conserved core of HIV-1 Nef complexed with a Src family SH3 domain

CH Lee, K Saksela, UA Mirza, BT Chait, J Kuriyan - Cell, 1996 - cell.com
The crystal structure of the conserved core of HIV-1 Nef has been determined in complex
with the SH3 domain of a mutant Fyn tyrosine kinase (a single amino acid substitution, Arg …

Exploiting the basis of proline recognition by SH3 and WW domains: design of N-substituted inhibitors

JT Nguyen, CW Turck, FE Cohen, RN Zuckermann… - Science, 1998 - science.org
Src homology 3 (SH3) and WW protein interaction domains bind specific proline-rich
sequences. However, instead of recognizing critical prolines on the basis of side chain …

DOCK180, a major CRK-binding protein, alters cell morphology upon translocation to the cell membrane

H Hasegawa, E Kiyokawa, S Tanaka… - … and cellular biology, 1996 - Taylor & Francis
CRK belongs to a family of adaptor proteins that consist mostly of SH2 and SH3 domains.
Far Western blotting with CRK SH3 has demonstrated that it binds to 135-to 145-, 160-, and …

ASAP1, a phospholipid-dependent arf GTPase-activating protein that associates with and is phosphorylated by Src

MT Brown, J Andrade, H Radhakrishna… - … and cellular biology, 1998 - Am Soc Microbiol
Membrane trafficking is regulated in part by small GTP-binding proteins of the ADP-
ribosylation factor (Arf) family. Arf function depends on the controlled exchange and …