Calmodulin interactions with Cav1 and Cav2 voltage-gated calcium channel IQ domains

نویسندگان

  • Eun Young Kim
  • Felix Findeisen
  • Daniel L Minor
چکیده

† Cardiovascular Research Institute, University of California, San Francisco, CA 94158-2330, USA ‡ Departments of Biochemistry and Biophysics, and Cellular and Molecular Pharmacology, University of California, San Francisco, CA 94158-2330, USA § California Institute for Quantitative Biomedical Research, University of California, San Francisco, CA 94158-2330, USA §§ Physical Biosciences Division, Lawrence Berkeley National Laboratory, Berkeley, CA 94720, USA

برای دانلود رایگان متن کامل این مقاله و بیش از 32 میلیون مقاله دیگر ابتدا ثبت نام کنید

ثبت نام

اگر عضو سایت هستید لطفا وارد حساب کاربری خود شوید

منابع مشابه

Apo states of calmodulin and CaBP1 control CaV1 voltage-gated calcium channel function through direct competition for the IQ domain.

In neurons, binding of calmodulin (CaM) or calcium-binding protein 1 (CaBP1) to the CaV1 (L-type) voltage-gated calcium channel IQ domain endows the channel with diametrically opposed properties. CaM causes calcium-dependent inactivation and limits calcium entry, whereas CaBP1 blocks calcium-dependent inactivation (CDI) and allows sustained calcium influx. Here, we combine isothermal titration ...

متن کامل

Calcium Channels Are Models of Self-Control

When Ca2+ ions fl ow through the pore of an individual voltage-gated Ca2+ channel, they act back on the channel they’ve passed through and alter subsequent Ca2+ fl ow. Such local, almost instantaneous regulation involves both positive and negative feedback mechanisms: Ca2+-dependent facilitation (CDF) and Ca2+-dependent inactivation (CDI), respectively. Indeed, some types of Ca2+ channel are ca...

متن کامل

Bio-Inspired Voltage-Dependent Calcium Channel Blockers

Ca(2+) influx via voltage-dependent CaV1/CaV2 channels couples electrical signals to biological responses in excitable cells. CaV1/CaV2 channel blockers have broad biotechnological and therapeutic applications. Here we report a general method for developing novel genetically encoded calcium channel blockers inspired by Rem, a small G-protein that constitutively inhibits CaV1/CaV2 channels. We s...

متن کامل

Structures of CaV2 Ca2+/CaM-IQ domain complexes reveal binding modes that underlie calcium-dependent inactivation and facilitation.

Calcium influx drives two opposing voltage-activated calcium channel (Ca(V)) self-modulatory processes: calcium-dependent inactivation (CDI) and calcium-dependent facilitation (CDF). Specific Ca(2+)/calmodulin (Ca(2+)/CaM) lobes produce CDI and CDF through interactions with the Ca(V)alpha(1) subunit IQ domain. Curiously, Ca(2+)/CaM lobe modulation polarity appears inverted between Ca(V)1s and C...

متن کامل

Molecular endpoints of Ca/calmodulin- and voltage-dependent inactivation of Cav1.3 channels

Ca entry through high voltage–gated Ca (CaV1 and CaV2) channels selectively triggers numerous neurobiological processes, including transmitter release, gene transcription, and memory formation (Berridge et al., 2000). Fitting with these vital roles, CaV1/2 channels are highly regulated through a variety of feedback mechanisms that inactivate channels in response to either intracellular Ca eleva...

متن کامل

ذخیره در منابع من


  با ذخیره ی این منبع در منابع من، دسترسی به آن را برای استفاده های بعدی آسان تر کنید

عنوان ژورنال:

دوره   شماره 

صفحات  -

تاریخ انتشار 2011