ArticleThe Journal of biological chemistry2014
Second transmembrane helix (M2) and long range coupling in Ca²⁺-ATPase.
Article in The Journal of biological chemistry, 2014. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 6 papers.
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Who cites it
6 citing papers in PubMed.
- Structural and energetic analysis of metastable intermediate states in the E1P-E2P transition of CaProceedings of the National Academy of Sciences of the United States of America · 2021Article
- Angle change of the A-domain in a single SERCA1a molecule detected by defocused orientation imaging.Scientific reports · 2021Article
- Membrane Perturbation of ADP-insensitive Phosphoenzyme of CaScientific reports · 2017Article
- Glycine 105 as Pivot for a Critical Knee-like Joint between Cytoplasmic and Transmembrane Segments of the Second Transmembrane Helix in Ca2+-ATPase.The Journal of biological chemistry · 2016Article
- Sarcolipin Promotes Uncoupling of the SERCA CaBiochemistry · 2016Article
- The N Terminus of Sarcolipin Plays an Important Role in Uncoupling Sarco-endoplasmic Reticulum Ca2+-ATPase (SERCA) ATP Hydrolysis from Ca2+ Transport.The Journal of biological chemistry · 2015Article
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Authors and funding
4 authors.
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Abstract
The actuator (A) domain of sarco(endo)plasmic reticulum Ca(2+)-ATPase not only plays a catalytic role but also undergoes large rotational movements that influence the distant transport sites through connections with transmembrane helices M1 and M2. Here we explore the importance of long helix M2 and its junction with the A domain by disrupting the helix structure and elongating with insertions of five glycine residues. Insertions into the membrane region of M2 and the top junctional segment impair Ca(2+) transport despite reasonable ATPase activity, indicating that they are uncoupled. These mutants fail to occlude Ca(2+). Those at the top segment also exhibited accelerated phosphoenzyme isomerization E1P → E2P. Insertions into the middle of M2 markedly accelerate E2P hydrolysis and cause strong resistance to inhibition by luminal Ca(2+). Insertions along almost the entire M2 region inhibit the dephosphorylated enzyme transition E2 → E1. The results pinpoint which parts of M2 control cytoplasm gating and which are critical for luminal gating at each stage in the transport cycle and suggest that proper gate function requires appropriate interactions, tension, and/or rigidity in the M2 region at appropriate times for coupling with A domain movements and catalysis.
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