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. 2021 May 26;9:688388. doi: 10.3389/fcell.2021.688388

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Copyright © 2021 Alfaidi, Scott and Orr.

This is an open-access article distributed under the terms of the Creative Commons Attribution License (CC BY). The use, distribution or reproduction in other forums is permitted, provided the original author(s) and the copyright owner(s) are credited and that the original publication in this journal is cited, in accordance with accepted academic practice. No use, distribution or reproduction is permitted which does not comply with these terms.

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Proposed model for Nck1/2 regulation. (A) Intramolecular interactions between the Nck1/2 SH3.2 domain and a peptide in the linker between the SH3.1 and SH3.2 domains may limit SH3.2 interactions with other targets. (B,C) Phosphorylation of Ser85 in response to cell stimulation may reduce this intramolecular interaction to activate Nck1/2, allowing recruitment of effector proteins. (D) Tyrosine phosphorylation within the WPY motifs in the SH3 domains may limit SH3 domain interactions to inactivate Nck1/2.