Open AccessANKRD54 preferentially selects Bruton’s Tyrosine Kinase (BTK) from a Human Src-Homology 3 (SH3) domain library
Author(s) -
Manuela O. Gustafsson,
Mohammad H Forouzanfar,
Erkko Ylösmäki,
Hyunseok Choi,
Subhash Shrestha,
Qing Wang,
Beston F. Nore,
Kalle Saksela,
Smith Rjh
Publication year - 2017
Publication title -
plos one
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 0.99
H-Index - 332
ISSN - 1932-6203
DOI - 10.1371/journal.pone.0174909
Subject(s) - bruton's tyrosine kinase , sh3 domain , proto oncogene tyrosine protein kinase src , tyrosine kinase , ankyrin repeat , interactome , protein kinase domain , biology , grb2 , microbiology and biotechnology , computational biology , kinase , genetics , signal transduction , gene , mutant
Bruton’s Tyrosine Kinase (BTK) is a cytoplasmic protein tyrosine kinase with a fundamental role in B-lymphocyte development and activation. The nucleocytoplasmic shuttling of BTK is specifically modulated by the Ankyrin Repeat Domain 54 (ANKRD54) protein and the interaction is known to be exclusively SH3-dependent. To identify the spectrum of the ANKRD54 SH3-interactome, we applied phage-display screening of a library containing all the 296 human SH3 domains. The BTK-SH3 domain was the prime interactor. Quantitative western blotting analysis demonstrated the accuracy of the screening procedure. Revealing the spectrum and specificity of ANKRD54-interactome is a critical step toward functional analysis in cells and tissues.
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