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• W1963710494 abstract "The Kelch-like 1 protein (KLHL1) is a neuronal actin-binding protein that modulates calcium channel function. It increases the current density of <mml:math xmlns:mml=http://www.w3.org/1998/Math/MathML id=M1><mml:mrow><mml:msub><mml:mrow><mml:mtext>Ca</mml:mtext></mml:mrow><mml:mtext>v</mml:mtext></mml:msub></mml:mrow></mml:math>3.2 (<mml:math xmlns:mml=http://www.w3.org/1998/Math/MathML id=M2><mml:mrow><mml:msub><mml:mi>α</mml:mi><mml:mrow><mml:mn>1</mml:mn><mml:mtext>H</mml:mtext></mml:mrow></mml:msub></mml:mrow></mml:math>) calcium channels via direct interaction with <mml:math xmlns:mml=http://www.w3.org/1998/Math/MathML id=M3><mml:mrow><mml:msub><mml:mi>α</mml:mi><mml:mrow><mml:mn>1</mml:mn><mml:mtext>H</mml:mtext></mml:mrow></mml:msub></mml:mrow></mml:math> and actin-F, resulting in biophysical changes in <mml:math xmlns:mml=http://www.w3.org/1998/Math/MathML id=M4><mml:mrow><mml:msub><mml:mrow><mml:mtext>Ca</mml:mtext></mml:mrow><mml:mtext>v</mml:mtext></mml:msub></mml:mrow></mml:math>3.2 currents and an increase in recycling endosomal activity with subsequent increased <mml:math xmlns:mml=http://www.w3.org/1998/Math/MathML id=M5><mml:mrow><mml:msub><mml:mi>α</mml:mi><mml:mrow><mml:mn>1</mml:mn><mml:mtext>H</mml:mtext></mml:mrow></mml:msub></mml:mrow></mml:math> channel number at the plasma membrane. Interestingly, removal of the actin-binding Kelch motif (ΔKelch) prevents the increase in <mml:math xmlns:mml=http://www.w3.org/1998/Math/MathML id=M6><mml:mrow><mml:msub><mml:mrow><mml:mtext>Ca</mml:mtext></mml:mrow><mml:mtext>v</mml:mtext></mml:msub></mml:mrow></mml:math>3.2 current density seen with wild-type KLHL1 when tested with normal square pulse protocols but does not preclude the effect when tested using action potential waveforms (AP). Here, we dissected the kinetic properties of the AP waveform that confer the mutant Kelch the ability to interact with <mml:math xmlns:mml=http://www.w3.org/1998/Math/MathML id=M7><mml:mrow><mml:msub><mml:mrow><mml:mtext>Ca</mml:mtext></mml:mrow><mml:mtext>v</mml:mtext></mml:msub></mml:mrow></mml:math>3.2 and induce an increase in calcium influx. We modified the action potential waveform by altering the slopes of repolarization and/or recovery from hyperpolarization or by changing the duration of the depolarization plateau or the hyperpolarization phase and tested the modulation of <mml:math xmlns:mml=http://www.w3.org/1998/Math/MathML id=M8><mml:mrow><mml:msub><mml:mrow><mml:mtext>Ca</mml:mtext></mml:mrow><mml:mtext>v</mml:mtext></mml:msub></mml:mrow></mml:math>3.2 by the mutant ΔKelch. Our results show that the recovery phase from hyperpolarization phase determines the conformational changes that allow the <mml:math xmlns:mml=http://www.w3.org/1998/Math/MathML id=M9><mml:mrow><mml:msub><mml:mi>α</mml:mi><mml:mrow><mml:mn>1</mml:mn><mml:mtext>H</mml:mtext></mml:mrow></mml:msub></mml:mrow></mml:math> subunit to properly interact with mutant KLHL1 lacking its actin-binding Kelch domains, leading to increased Ca influx." @default.
• W1963710494 created "2016-06-24" @default.
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• W1963710494 date "2012-07-11" @default.
• W1963710494 modified "2023-10-15" @default.
• W1963710494 title "Elimination of the Actin-Binding Domain in Kelch-Like 1 Protein Induces T-Type Calcium Channel Modulation Only in the Presence of Action Potential Waveforms" @default.
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• W1963710494 doi "https://doi.org/10.1155/2012/505346" @default.
• W1963710494 hasPubMedCentralId "https://www.ncbi.nlm.nih.gov/pmc/articles/3401526" @default.
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