Annexin A2-S100A10 Represents the Regulatory Component of Maxi-Cl Channel Dependent on Protein Tyrosine Dephosphorylation and Intracellular Ca²⁺
Md. Rafiqul IslamDivision of Cell Signaling, National Institute for Physiological Sciences (NIPS), Okazaki, JapanToshiaki OkadaDivision of Cell Signaling, National Institute for Physiological Sciences (NIPS), Okazaki, JapanPetr G. MerzlyakDivision of Cell Signaling, National Institute for Physiological Sciences (NIPS), Okazaki, JapanAbduqodir ToychievDepartment of Biological Sciences, State University of New York College of Optometry, New York, NY, USAYuhko Ando‐AkatsukaDepartment of Cell Physiology, Faculty of Pharmaceutical Sciences, Suzuka University of Medical Science, Suzuka, JapanRavshan Z. SabirovDivision of Cell Signaling, National Institute for Physiological Sciences (NIPS), Okazaki, JapanYasunobu OkadaDepartment of Physiology, Kyoto Prefectural University of Medicine, Kyoto, Japan
ABI
Аннотация
BACKGROUND/AIMS: Maxi-anion channel (Maxi-Cl) is ubiquitously expressed and involved in a number of important cell functions especially by serving as an ATP release pathway. We recently identified SLCO2A1 as its essential core component. However, the regulatory component required for the channel activation/inactivation remains unidentified. METHODS: In the present study, to identify the regulatory component, we made genome-wide analysis combined with siRNA screening and performed patch-clamp studies and ATP release assay after gene silencing and overexpression. RESULTS: dependence of Maxi-Cl activity was abolished by S100a10 knockdown. CONCLUSION: sensitivity on this channel.
Перевод пока недоступен
Темы
Идентификаторы
Цитирования и источники
Цитирований: 4Использованных источников: 0