In smooth muscle, calcium binding to calmodulin activates myosin light chain kinase (MLCK). What is the mechanism by which the calcium-calmodulin complex activates MLCK?
- A Causes dimerization of MLCK
- B Translocates MLCK to the plasma membrane
- C Phosphorylates MLCK at a regulatory site
- D Removes an autoinhibitory domain from MLCK ✓
Correct answer: D. Removes an autoinhibitory domain from MLCK
Explanation
MLCK is maintained inactive by an autoinhibitory domain that blocks the catalytic site. When Ca2+-calmodulin binds to MLCK, it displaces this autoinhibitory domain, allowing the kinase to phosphorylate myosin light chains and initiate contraction. This is direct allosteric activation, not phosphorylation or dimerization.
Reference: Lehninger Principles of Biochemistry, 7th ed.
High-yield for: NEET PGINI-CETNExTFMGEUSMLEPLABMRCP
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