ANKRD54 preferentially selects Bruton's Tyrosine Kinase (BTK) from a Human Src-Homology 3 (SH3) domain library.
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 exclu...
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doaj-bce0773e704f4ae98bda97980d431bb92020-11-25T02:47:26ZengPublic Library of Science (PLoS)PLoS ONE1932-62032017-01-01124e017490910.1371/journal.pone.0174909ANKRD54 preferentially selects Bruton's Tyrosine Kinase (BTK) from a Human Src-Homology 3 (SH3) domain library.Manuela O GustafssonDara K MohammadErkko YlösmäkiHyunseok ChoiSubhash ShresthaQing WangBeston F NoreKalle SakselaC I Edvard SmithBruton'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.http://europepmc.org/articles/PMC5378395?pdf=render |
collection |
DOAJ |
language |
English |
format |
Article |
sources |
DOAJ |
author |
Manuela O Gustafsson Dara K Mohammad Erkko Ylösmäki Hyunseok Choi Subhash Shrestha Qing Wang Beston F Nore Kalle Saksela C I Edvard Smith |
spellingShingle |
Manuela O Gustafsson Dara K Mohammad Erkko Ylösmäki Hyunseok Choi Subhash Shrestha Qing Wang Beston F Nore Kalle Saksela C I Edvard Smith ANKRD54 preferentially selects Bruton's Tyrosine Kinase (BTK) from a Human Src-Homology 3 (SH3) domain library. PLoS ONE |
author_facet |
Manuela O Gustafsson Dara K Mohammad Erkko Ylösmäki Hyunseok Choi Subhash Shrestha Qing Wang Beston F Nore Kalle Saksela C I Edvard Smith |
author_sort |
Manuela O Gustafsson |
title |
ANKRD54 preferentially selects Bruton's Tyrosine Kinase (BTK) from a Human Src-Homology 3 (SH3) domain library. |
title_short |
ANKRD54 preferentially selects Bruton's Tyrosine Kinase (BTK) from a Human Src-Homology 3 (SH3) domain library. |
title_full |
ANKRD54 preferentially selects Bruton's Tyrosine Kinase (BTK) from a Human Src-Homology 3 (SH3) domain library. |
title_fullStr |
ANKRD54 preferentially selects Bruton's Tyrosine Kinase (BTK) from a Human Src-Homology 3 (SH3) domain library. |
title_full_unstemmed |
ANKRD54 preferentially selects Bruton's Tyrosine Kinase (BTK) from a Human Src-Homology 3 (SH3) domain library. |
title_sort |
ankrd54 preferentially selects bruton's tyrosine kinase (btk) from a human src-homology 3 (sh3) domain library. |
publisher |
Public Library of Science (PLoS) |
series |
PLoS ONE |
issn |
1932-6203 |
publishDate |
2017-01-01 |
description |
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. |
url |
http://europepmc.org/articles/PMC5378395?pdf=render |
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