Structural and functional conservation of the activating Ca2+ binding site in inositol 1,4.5-trisphosphate and ryanodine receptors.

肌醇 1, 4.5 - 三磷酸和 ryanodine 受体中激活 Ca2 结合位点的结构和功能保守性。

• 影响指数: 4.69
• 发表时间: 12 2022
• 来源期刊: Cell Calcium
• DOI: 10.1016/j.ceca.2022.102671
• PMID: 36370621
• 文章类型: Journal Article
• 中科院分区: Q2
• 方向: 生物
• 作者列表: Chen YS,Van Petegem F

关键词: Calcium binding site; Calcium release channels; Calcium signaling; Inositol 1,4,5-trisphosphate receptor; Ryanodine receptor

Mesh: Ryanodine Receptor Calcium Release Channel / metabolism; Inositol 1,4,5-Trisphosphate Receptors / metabolism; Inositol / metabolism; Sarcoplasmic Reticulum / metabolism; Binding Sites; Calcium / metabolism; Calcium Signaling; Inositol 1,4,5-Trisphosphate / metabolism

Abstract

Inositol 1,4,5-trisphosphate receptors (IP3Rs) and Ryanodine Receptors (RyRs) dictate the release of Ca2+ from the Endoplasmic (ER) and Sarcoplasmic Reticulum (SR). Arige et al [1] investigated the functional importance of specific Ca2+-coordinating residues, unambiguously confirming the activating Ca2+ binding site in the IP3R.

摘要

肌醇1,4,5-三磷酸受体（IP3R）和Ryanodine受体（RyR）决定了Ca2从内质网（ER）和肌浆网（SR）的释放。Arige等人[1]研究了特定Ca2+配位残基的功能重要性，明确确认IP3R中激活的Ca2+结合位点。