ANKRD54 preferentially selects Bruton's Tyrosine Kinase (BTK) from a Human Src-Homology 3 (SH3) domain library

Manuela O Gustafsson; Dara K Mohammad; Erkko Ylösmäki; Hyunseok Choi; Subhash Shrestha; Qing Wang; Beston F Nore; Kalle Saksela; C I Edvard Smith

doi:10.1371/journal.pone.0174909

ANKRD54 preferentially selects Bruton's Tyrosine Kinase (BTK) from a Human Src-Homology 3 (SH3) domain library

PLoS One. 2017 Apr 3;12(4):e0174909. doi: 10.1371/journal.pone.0174909. eCollection 2017.

Authors

Affiliations

¹ Department of Laboratory Medicine, Clinical Research Center, Karolinska Institutet, Karolinska University Hospital Huddinge, SE Stockholm, Sweden.
² Department of Biology, College of Science, Salahaddin University-Erbil, Erbil, Kurdistan Region-Iraq.
³ Department of Virology, University of Helsinki and Helsinki University Hospital, Helsinki, Finland.
⁴ Department of Biochemistry, School of Medicine, Faculty of Medical Sciences, University of Sulaimani, Sulaimani, Iraq.
⁵ Department of Health, Kurdistan Institution for Strategic Studies and Scientific Research (KISSSR), Sulaimani, Kurdistan-Iraq.

Abstract

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.

MeSH terms

Agammaglobulinaemia Tyrosine Kinase
Animals
B-Lymphocytes / cytology
COS Cells
Cell Line, Tumor
Chlorocebus aethiops
HEK293 Cells
Humans
Mutation / genetics
Nuclear Proteins / genetics
Nuclear Proteins / metabolism*
Peptide Library
Protein Binding / genetics
Protein-Tyrosine Kinases / genetics
Protein-Tyrosine Kinases / metabolism*
Signal Transduction
src Homology Domains / genetics
src Homology Domains / physiology*

Substances

ANKRD54 protein, human
Nuclear Proteins
Peptide Library
Protein-Tyrosine Kinases
Agammaglobulinaemia Tyrosine Kinase
BTK protein, human

Grants and funding

MOG holds a Ph.D. scholarship from Södertörn University-College, Sweden. DKM maintains a postdoctoral-fellowship from MoHE in the Kurdistan-Regional Government, Iraq. The project was supported by a grant from the Swedish Cancer Society.