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Characterization of ATPase Activity of P2RX2 Cation Channel.
Mittal, Rahul; Grati, M'hamed; Sedlacek, Miloslav; Yuan, Fenghua; Chang, Qing; Yan, Denise; Lin, Xi; Kachar, Bechara; Farooq, Amjad; Chapagain, Prem; Zhang, Yanbin; Liu, Xue Z.
Afiliación
  • Mittal R; Department of Otolaryngology, University of Miami Miller School of Medicine Miami, FL, USA.
  • Grati M; Department of Otolaryngology, University of Miami Miller School of Medicine Miami, FL, USA.
  • Sedlacek M; Laboratory of Cell Structure and Dynamics, Section on Structural Cell Biology, National Institute on Deafness and Other Communication Disorders, National Institutes of Health Bethesda, MD, USA.
  • Yuan F; Department of Biochemistry, University of Miami Leonard M. Miller School of Medicine Miami, FL, USA.
  • Chang Q; Department of Otolaryngology, Emory University Atlanta, GA, USA.
  • Yan D; Department of Otolaryngology, University of Miami Miller School of Medicine Miami, FL, USA.
  • Lin X; Department of Otolaryngology, Emory University Atlanta, GA, USA.
  • Kachar B; Laboratory of Cell Structure and Dynamics, Section on Structural Cell Biology, National Institute on Deafness and Other Communication Disorders, National Institutes of Health Bethesda, MD, USA.
  • Farooq A; Department of Biochemistry, University of Miami Leonard M. Miller School of Medicine Miami, FL, USA.
  • Chapagain P; Department of Physics, Florida International University Miami, FL, USA.
  • Zhang Y; Department of Biochemistry, University of Miami Leonard M. Miller School of Medicine Miami, FL, USA.
  • Liu XZ; Department of Otolaryngology, University of Miami Miller School of MedicineMiami, FL, USA; Department of Biochemistry, University of Miami Leonard M. Miller School of MedicineMiami, FL, USA; Department of Otolaryngology, Central South University, Xiangya HospitalChangsha, China.
Front Physiol ; 7: 186, 2016.
Article en En | MEDLINE | ID: mdl-27252659
P2X purinergic receptors are plasma membrane ATP-dependent cation channels that are broadly distributed in the mammalian tissues. P2RX2 is a modulator of auditory sensory hair cell mechanotransduction and plays an important role in hair cell tolerance to noise. In this study, we demonstrate for the first time in vitro and in cochlear neuroepithelium, that P2RX2 possesses the ATPase activity. We observed that the P2RX2 V60L human deafness mutation alters its ability to bind ATP, while the G353R has no effect on ATP binding or hydrolysis. A non-hydrolysable ATP assay using HEK293 cells suggests that ATP hydrolysis plays a significant role in the opening and gating of the P2RX2 ion channel. Moreover, the results of structural modeling of the molecule was in agreement with our experimental observations. These novel findings suggest the intrinsic ATPase activity of P2RX2 and provide molecular insights into the channel opening.
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Texto completo: 1 Colección: 01-internacional Base de datos: MEDLINE Tipo de estudio: Prognostic_studies Idioma: En Revista: Front Physiol Año: 2016 Tipo del documento: Article País de afiliación: Estados Unidos Pais de publicación: Suiza
Texto completo
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Texto completo: 1 Colección: 01-internacional Base de datos: MEDLINE Tipo de estudio: Prognostic_studies Idioma: En Revista: Front Physiol Año: 2016 Tipo del documento: Article País de afiliación: Estados Unidos Pais de publicación: Suiza