Calmodulin regulates Ca2+-dependent feedback inhibition of store-operated Ca2+ influx by interaction with a site in the C terminus of TrpC1

Brij B. Singh; Xibao Liu; Jisen Tang; Michael X. Zhu; Indu S. Ambudkar

doi:10.1016/S1097-2765(02)00506-3

Calmodulin regulates Ca²⁺-dependent feedback inhibition of store-operated Ca²⁺ influx by interaction with a site in the C terminus of TrpC1

Brij B. Singh, Xibao Liu, Jisen Tang, Michael X. Zhu, Indu S. Ambudkar

School of Dentistry

Research output: Contribution to journal › Article

116 Scopus citations

Abstract

The mechanism involved in [Ca²⁺]_i-dependent feedback inhibition of store-operated Ca²⁺ entry (SOCE) is not yet known. Expression of Ca²⁺-insensitive calmodulin (Mut-CaM) but not wild-type CaM increased SOCE and decreased its Ca²⁺-dependent inactivation. Expression of TrpC1 lacking C terminus aa 664-793 (TrpC1ΔC) also attenuated Ca²⁺-dependent inactivation of SOCE. CaM interacted with endogenous and expressed TrpC1 and with GST-TrpC1 C terminus but not with TrpC1ΔC. Two CaM binding domains, aa 715-749 and aa 758-793, were identified. Expression of TrpC1Δ758-793 but not TrpC1Δ715-749 mimicked the effects of TrpC1ΔC and Mut-CaM on SOCE. These data demonstrate that CaM mediates Ca²⁺-dependent feedback inhibition of SOCE via binding to a domain in the C terminus of TrpC1. These findings reveal an integral role for TrpC1 in the regulation of SOCE.

Original language	English (US)
Pages (from-to)	739-750
Number of pages	12
Journal	Molecular Cell
Volume	9
Issue number	4
DOIs	https://doi.org/10.1016/S1097-2765(02)00506-3
State	Published - Jan 1 2002

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ASJC Scopus subject areas

Molecular Biology
Cell Biology

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Singh, B. B., Liu, X., Tang, J., Zhu, M. X., & Ambudkar, I. S. (2002). Calmodulin regulates Ca²⁺-dependent feedback inhibition of store-operated Ca²⁺ influx by interaction with a site in the C terminus of TrpC1. Molecular Cell, 9(4), 739-750. https://doi.org/10.1016/S1097-2765(02)00506-3

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abstract = "The mechanism involved in [Ca2+]i-dependent feedback inhibition of store-operated Ca2+ entry (SOCE) is not yet known. Expression of Ca2+-insensitive calmodulin (Mut-CaM) but not wild-type CaM increased SOCE and decreased its Ca2+-dependent inactivation. Expression of TrpC1 lacking C terminus aa 664-793 (TrpC1ΔC) also attenuated Ca2+-dependent inactivation of SOCE. CaM interacted with endogenous and expressed TrpC1 and with GST-TrpC1 C terminus but not with TrpC1ΔC. Two CaM binding domains, aa 715-749 and aa 758-793, were identified. Expression of TrpC1Δ758-793 but not TrpC1Δ715-749 mimicked the effects of TrpC1ΔC and Mut-CaM on SOCE. These data demonstrate that CaM mediates Ca2+-dependent feedback inhibition of SOCE via binding to a domain in the C terminus of TrpC1. These findings reveal an integral role for TrpC1 in the regulation of SOCE.",

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N2 - The mechanism involved in [Ca2+]i-dependent feedback inhibition of store-operated Ca2+ entry (SOCE) is not yet known. Expression of Ca2+-insensitive calmodulin (Mut-CaM) but not wild-type CaM increased SOCE and decreased its Ca2+-dependent inactivation. Expression of TrpC1 lacking C terminus aa 664-793 (TrpC1ΔC) also attenuated Ca2+-dependent inactivation of SOCE. CaM interacted with endogenous and expressed TrpC1 and with GST-TrpC1 C terminus but not with TrpC1ΔC. Two CaM binding domains, aa 715-749 and aa 758-793, were identified. Expression of TrpC1Δ758-793 but not TrpC1Δ715-749 mimicked the effects of TrpC1ΔC and Mut-CaM on SOCE. These data demonstrate that CaM mediates Ca2+-dependent feedback inhibition of SOCE via binding to a domain in the C terminus of TrpC1. These findings reveal an integral role for TrpC1 in the regulation of SOCE.

AB - The mechanism involved in [Ca2+]i-dependent feedback inhibition of store-operated Ca2+ entry (SOCE) is not yet known. Expression of Ca2+-insensitive calmodulin (Mut-CaM) but not wild-type CaM increased SOCE and decreased its Ca2+-dependent inactivation. Expression of TrpC1 lacking C terminus aa 664-793 (TrpC1ΔC) also attenuated Ca2+-dependent inactivation of SOCE. CaM interacted with endogenous and expressed TrpC1 and with GST-TrpC1 C terminus but not with TrpC1ΔC. Two CaM binding domains, aa 715-749 and aa 758-793, were identified. Expression of TrpC1Δ758-793 but not TrpC1Δ715-749 mimicked the effects of TrpC1ΔC and Mut-CaM on SOCE. These data demonstrate that CaM mediates Ca2+-dependent feedback inhibition of SOCE via binding to a domain in the C terminus of TrpC1. These findings reveal an integral role for TrpC1 in the regulation of SOCE.

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10.1016/S1097-2765(02)00506-3