Orchestration of ErbB3 signaling through heterointeractions and homointeractions

McCabe Pryor, Meghan; Steinkamp, Mara P.; Halasz, Adam M.; Chen, Ye; Yang, Shujie; Smith, Marilyn S.; Zahoransky-Kohalmi, Gergely; Swift, Mark; Xu, Xiao-Ping; Hanien, Dorit; Volkmann, Niels; Lidke, Diane S.; Edwards, Jeremy S.; Wilson, Bridget S.

doi:10.1091/mbc.e14-06-1114

Orchestration of ErbB3 signaling through heterointeractions and homointeractions

Journal Article · Wed Sep 16 00:00:00 EDT 2015 · Molecular Biology of the Cell

DOI:https://doi.org/10.1091/mbc.e14-06-1114· OSTI ID:1625236

McCabe Pryor, Meghan ^[1]; Steinkamp, Mara P. ^[2]; Halasz, Adam M. ^[3]; Chen, Ye ^[3]; Yang, Shujie ^[4]; Smith, Marilyn S. ^[5]; Zahoransky-Kohalmi, Gergely ^[6]; Swift, Mark ^[7]; Xu, Xiao-Ping ^[7]; Hanien, Dorit ^[7]; Volkmann, Niels ^[7]; Lidke, Diane S. ^[2]; Edwards, Jeremy S. ^[8]; Wilson, Bridget S. ^[2]

Univ. of New Mexico, Albuquerque, NM (United States). Dept. of Chemical and Biological Engineering; Los Alamos National Lab. (LANL), Los Alamos, NM (United States). Center for Nonlinear Studies; DOE/OSTI
Univ. of New Mexico, Albuquerque, NM (United States). Dept. of Pathology; Univ. of New Mexico, Albuquerque, NM (United States). Univ. of New Mexico Health Sciences Center. Cancer Center
West Virginia Univ., Morgantown, WV (United States). Dept. of Mathematics
Univ. of Iowa, Iowa City, IA (United States). Carver College of Medicine. Dept. of OB/GYN
Viracor-IBT Labs, Lee’s Summit, MO (United States)
Univ. of New Mexico, Albuquerque, NM (United States). Dept. of Pathology
Sanford-Burnham Medical Research Institute, La Jolla, CA (United States). Bioinformatics and Systems Biology Program
Univ. of New Mexico, Albuquerque, NM (United States). Dept. of Chemical and Biological Engineering; Univ. of New Mexico, Albuquerque, NM (United States). Univ. of New Mexico Health Sciences Center. Cancer Center; Univ. of New Mexico, Albuquerque, NM (United States). Dept. of Chemistry and Chemical Biology

Members of the ErbB family of receptor tyrosine kinases are capable of both homointeractions and heterointeractions. Because each receptor has a unique set of binding sites for downstream signaling partners and differential catalytic activity, subtle shifts in their combinatorial interplay may have a large effect on signaling outcomes. The overexpression and mutation of ErbB family members are common in numerous human cancers and shift the balance of activation within the signaling network. Here we report the development of a spatial stochastic model that addresses the dynamics of ErbB3 homodimerization and heterodimerization with ErbB2. The model is based on experimental measures for diffusion, dimer off-rates, kinase activity, and dephosphorylation. We also report computational analysis of ErbB3 mutations, generating the prediction that activating mutations in the intracellular and extracellular domains may be subdivided into classes with distinct underlying mechanisms. We show experimental evidence for an ErbB3 gain-of-function point mutation located in the C-lobe asymmetric dimerization interface, which shows enhanced phosphorylation at low ligand dose associated with increased kinase activity.

View Accepted Manuscript (DOE)

Research Organization:: Los Alamos National Laboratory (LANL), Los Alamos, NM (United States)

Sponsoring Organization:: USDOE Office of Science (SC), Biological and Environmental Research (BER). Biological Systems Science Division

Grant/Contract Number:: AC52-06NA25396

OSTI ID:: 1625236

Journal Information:: Molecular Biology of the Cell, Journal Name: Molecular Biology of the Cell Journal Issue: 22 Vol. 26; ISSN 1059-1524

Publisher:: American Society for Cell BiologyCopyright Statement

Country of Publication:: United States

Language:: English

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