Open AccessA synergy between mechanosensitive calcium- and membrane-binding mediates tension-sensing by C2-like domains
Author(s) -
Zhouyang Shen,
Kalina T. Belcheva,
Mark Jelcic,
King Lam Hui,
Anushka Katikaneni,
Philipp Niethammer
Publication year - 2021
Publication title -
proceedings of the national academy of sciences of the united states of america
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 5.011
H-Index - 771
eISSN - 1091-6490
pISSN - 0027-8424
DOI - 10.1073/pnas.2112390119
Subject(s) - mechanosensitive channels , mechanotransduction , membrane , c2 domain , biophysics , chemistry , microbiology and biotechnology , biology , biochemistry , ion channel , receptor
Significance A cell must be able to measure whether the lipid membranes that surround its insides are stretched. Currently, mechanosensitive ion channels are the best-studied class of membrane tension sensors, but recent work suggests that peripheral membrane enzymes that gauge nuclear confinement or swelling during cell migration or upon tissue injury constitute a second class. The mechanosensitivity of these enzymes derives from their calcium-dependent (“C2-like”) membrane-interaction domains. Although these can be found in many important signaling proteins, they have remained virtually unstudied as mechanotransducers. How membrane tension controls these domains and what features render them mechanosensitive is unclear. Here, we show that membrane tension-sensing by C2-like domains is mediated by a synergy between mechanosensitive calcium-binding and membrane insertion.