TY - JOUR
T1 - Calcium-modulated ciliary membrane guanylate cyclase transduction machinery
T2 - Constitution and operational principles
AU - Duda, Teresa
AU - Fik-Rymarkiewicz, Ewa
AU - Venkataraman, Venkateswar
AU - Krishnan, Anuradha
AU - Sharma, Rameshwar K.
N1 - Funding Information:
This study was supported by the USPHS awards DC 005349 and EY 10828 (R.K.S.), HL 070015 (T.D.) and an intramural grant AG00925 (V.V); by the affiliated support of the Research to Prevent Blindness Inc., New York and the Lions Eye Research Foundation, New Jersey.
PY - 2004/12
Y1 - 2004/12
N2 - Odorant transduction is a biochemical process by which the odorant signal generates the electric signal. The cilia of the olfactory neuroepithelium are the sites of this process. This study documents the detailed biochemical, structural and functional description of an odorant-responsive Ca2+-modulated membrane guanylate cyclase transduction machinery in the cilia. Myristoylated (myr)-neurocalcin δ is the Ca2+-sensor component and the cyclase, ONE-GC, the transduction component of the machinery. Myr-neurocalcin δ senses increments in free Ca2+, binds to a defined domain of ONE-GC and stimulates the cyclase. The findings enable the formulation of an odorant transduction model in which three pivotal signaling components - Ca2+, myr-neurocalcin δ and ONE-GC - of the transduction machinery are locked. A glaring feature of the model is that its Ca2+-dependent operational principle is opposite to the phototransduction model.
AB - Odorant transduction is a biochemical process by which the odorant signal generates the electric signal. The cilia of the olfactory neuroepithelium are the sites of this process. This study documents the detailed biochemical, structural and functional description of an odorant-responsive Ca2+-modulated membrane guanylate cyclase transduction machinery in the cilia. Myristoylated (myr)-neurocalcin δ is the Ca2+-sensor component and the cyclase, ONE-GC, the transduction component of the machinery. Myr-neurocalcin δ senses increments in free Ca2+, binds to a defined domain of ONE-GC and stimulates the cyclase. The findings enable the formulation of an odorant transduction model in which three pivotal signaling components - Ca2+, myr-neurocalcin δ and ONE-GC - of the transduction machinery are locked. A glaring feature of the model is that its Ca2+-dependent operational principle is opposite to the phototransduction model.
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U2 - 10.1023/B:MCBI.0000049372.33965.4f
DO - 10.1023/B:MCBI.0000049372.33965.4f
M3 - Article
C2 - 15663192
AN - SCOPUS:9444229934
SN - 0300-8177
VL - 267
SP - 107
EP - 122
JO - Molecular and cellular biochemistry
JF - Molecular and cellular biochemistry
IS - 1-2
ER -