Cloning and tissue‐specific expression of the brain calcium channel β‐subunit

Pragnell, Marlon; Sakamoto, Junshi; Jay, Scott D.; Campbell, Kevin P.

doi:10.1016/0014-5793(91)81296-k

Cited by 184 publications

(110 citation statements)

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“…cDNAs encoding the wild-type ␣ 1 1.2, ␤ 1b , and ␣ 2 ␦ subunits (5,(26)(27)(28) were subcloned into the pCDNA3.1 vector (Stratagene). The mutants were created by using overlap extension PCR mutagenesis with PFU Turbo (Stratagene).…”

Section: Methodsmentioning

confidence: 99%

“…tsA-201 cells were grown to 90% confluence, suspended with trypsin͞EDTA, and plated onto 35-mm culture dishes (Corning) at 40% confluence 24 h before transfection. Immediately before transfection, the medium was replaced with fresh DMEM͞F-12 supplemented with serum and antibiotics, and the cells were transiently transfected with cDNAs encoding rabbit cardiac ␣ 1 1.2 (5) or rat brain ␣ 1 1.2 (26), ␤ 1b (27), and ␣ 2 ␦ 1 (28) subunits at a 1:1:1 molar ratio by using the calcium phosphate technique as described (29). In addition, cells were Abbreviations: PKC, protein kinase C; PMA, 4-␣-phorbol 12-myristate 13-acetate; OAG, rac-1-oleyl-2-acetylglycerol.…”

Section: Methodsmentioning

confidence: 99%

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Inhibition of cardiac L-type calcium channels by protein kinase C phosphorylation of two sites in the N-terminal domain

McHugh

Sharp

Scheuer

et al. 2000

Proc. Natl. Acad. Sci. U.S.A.

142

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We have investigated the mechanism underlying the modulation of the cardiac L-type Ca 2؉ current by protein kinase C (PKC). Using the patch-clamp technique, we found that PKC activation by 4-␣-phorbol 12-myristate 13-acetate (PMA) or rac-1-oleyl-2-acetylglycerol (OAG) caused a substantial reduction in Ba 2؉ current through Ca v1.2 channels composed of ␣11.2, ␤1b, and ␣2␦1 subunits expressed in tsA-201 cells. In contrast, Ba 2؉ current through a cloned brain isoform of the Ca v1.2 channel (rbC-II) was unaffected by PKC activation. Two potential sites of PKC phosphorylation are present at positions 27 and 31 in the cardiac form of Ca v1.2, but not in the brain form. Deletion of N-terminal residues 2-46 prevented PKC inhibition. Conversion of the threonines at positions 27 and 31 to alanine also abolished the PKC sensitivity of Ca v1.2. Mutant Cav1.2 channels in which the threonines were converted singly to alanines were also insensitive to PKC modulation, suggesting that phosphorylation of both residues is required for PKC-dependent modulation. Consistent with this, mutating each of the threonines individually to aspartate in separate mutants restored the PKC sensitivity of Ca v1.2, indicating that a change in net charge by phosphorylation of both sites is responsible for inhibition. Our results define the molecular basis for inhibition of cardiac Ca v1.2 channels by the PKC pathway.

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Section: Methodsmentioning

confidence: 99%

Section: Methodsmentioning

confidence: 99%

Inhibition of cardiac L-type calcium channels by protein kinase C phosphorylation of two sites in the N-terminal domain

McHugh

Sharp

Scheuer

et al. 2000

Proc. Natl. Acad. Sci. U.S.A.

142

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“…Mature X. laevis female frogs were from Nasco (Wisconsin, USA). The ~A subunit (pSPCBI-2) was from Mori et al [6] and thefll ~ clone from Pragnell et al [25].…”

Section: Methodsmentioning

confidence: 99%

Identification of critical amino acids involved in α₁‐β interaction in voltage‐dependent Ca²⁺ channels

et al. 1996

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In voltage-dependent Ca 2+ channels, the al and subunits interact via two cytoplasmic regions defined as the Alpha Interaction Domain (AID) and Beta Interaction Domain (BID). Several novel amino acids for that interaction have now been mapped in both domains by point mutations. It was found that three of the nine amino acids in AID and four of the eight BID amino acids tested were essential for the interaction. Whereas the important AID amino acids were clustered around five residues, the important BID residues were more widely distributed within a larger 16 amino acid sequence. The affinity of the AID A GST fusion protein for the four interacting/]lb BID mutants was not significantly altered compared with the wild-type ~b despite the close localization of mutated residues to disruptive BID amino acids. Expression of these interactive S] mutants with the fulllength OLIA subunit only slightly modified the stimulation efficiency when compared with the wild-type ~b subunit. Our data suggest that non-disruptive BID sequence alterations do not dramatically affect the/] subunit-induced current stimulation.

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“…Polyclonal antibodies Sheep 37, Sheep 46, Sheep 49, Rabbit 145, and Rabbit 239, specific for the neuronal Ca 2ϩ channel subunits ␣ 1 2.1͞2, ␣ 1 2.2, ␤ 3 , ␤ 4 , and ␥ 2/3 , respectively, have been described (6,(26)(27)(28). Antibodies IIID5E1, Guinea Pig 1, Sheep 6, and Guinea Pig 16, specific for the skeletal muscle Ca 2ϩ channel subunits ␣ 1 1.1, ␣ 2 ␦, ␤ 1a , and ␥ 1 , respectively, have been characterized (7,(29)(30)(31). Monoclonal antibody VD2 1 , which recognizes all Ca 2ϩ channel ␤ subunits, has been described (32).…”

Section: Methodsmentioning

confidence: 99%

A functional AMPA receptor–calcium channel complex in the postsynaptic membrane

Kang

Chen

Wakamori

et al. 2006

Proc. Natl. Acad. Sci. U.S.A.

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Ca 2؉ channels play critical roles in the regulation of synaptic activity. In contrast to the well established function of voltageactivated Ca 2؉ channels in the presynaptic membrane for neurotransmitter release, some studies are just beginning to elucidate the functions of the Ca 2؉ channels in the postsynaptic membrane.In this study, we demonstrated the functional association of ␣-amino-3-hydroxy-5-methyl-4-isoxazolepropionate (AMPA) receptors with the neuronal Ca 2؉ channels. A series of biochemical studies showed the specific association of Ca v2.1 (␣1A-class) and Ca v2.2 (␣1B-class) with AMPA receptors in the postsynaptic membrane. Our electrophysiological and Ca 2؉ imaging analyses of recombinant Ca v2.1 and AMPA receptors also showed functional coupling of the two channels. Considering the critical roles of postsynaptic intracellular concentration of Ca 2؉ ([Ca 2؉ ]i) increase and AMPA receptor trafficking for long-term potentiation (LTP) and long-term depression (LTD), the functional association of Ca 2؉ channels with the AMPA receptors may provide new insights into the mechanism of synaptic plasticity.voltage-activated Ca 2ϩ channel ͉ stargazin ͉ glutamate receptor ͉ synaptic plasticity ͉ postsynaptic density N eurotransmitter-mediated communication between a presynaptic and a postsynaptic membrane is a fundamental neurophysiological phenomenon. The precise organization and dynamic change of presynaptic and postsynaptic protein components underlies the physiological regulation of synaptic efficacy. The study of the organization and dynamics of synaptic proteins is the key to our understanding of synaptic plasticity, neuronal development, and some neurological disorders.The ␣-amino-3-hydroxy-5-methyl-4-isoxazolepropionate (AMPA) receptor is one of the major types of glutamate receptors (GluRs) mediating neurotransmission in the excitatory postsynaptic membrane. Activity-dependent trafficking of AMPA receptors in and out of the postsynaptic membrane is one of the key mechanisms for synaptic plasticity such as long-term potentiation (LTP) and long-term depression. Although recent studies have identified several postsynaptic proteins that interact with the AMPA receptor C terminus and are potentially involved in AMPA receptor trafficking, the precise mechanism for the modulation of AMPA receptors trafficking in the postsynaptic membrane is still not clear (1).Voltage-activated Ca 2ϩ channels function in many fundamental physiological processes, including neurotransmission, muscle contraction, intracellular signaling, hormone secretion, and development. The function of voltage-activated Ca 2ϩ channels (called Ca 2ϩ channels or Ca v hereafter) for neurotransmission in the presynaptic membrane has been intensively studied because the Ca 2ϩ channel is a key player in the coupling of electric and chemical signals in presynapses. In addition to the presynaptic function, postsynaptic function of Ca 2ϩ channels is beginning to be revealed through recent biophysical studies. Induction of hippocampal mossy fiber LTP ...

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Cloning and tissue‐specific expression of the brain calcium channel β‐subunit

Cited by 184 publications

References 28 publications

Inhibition of cardiac L-type calcium channels by protein kinase C phosphorylation of two sites in the N-terminal domain

Inhibition of cardiac L-type calcium channels by protein kinase C phosphorylation of two sites in the N-terminal domain

Identification of critical amino acids involved in α₁‐β interaction in voltage‐dependent Ca²⁺ channels

A functional AMPA receptor–calcium channel complex in the postsynaptic membrane

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Cloning and tissue‐specific expression of the brain calcium channel β‐subunit

Cited by 184 publications

References 28 publications

Inhibition of cardiac L-type calcium channels by protein kinase C phosphorylation of two sites in the N-terminal domain

Inhibition of cardiac L-type calcium channels by protein kinase C phosphorylation of two sites in the N-terminal domain

Identification of critical amino acids involved in α1‐β interaction in voltage‐dependent Ca2+ channels

A functional AMPA receptor–calcium channel complex in the postsynaptic membrane

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Identification of critical amino acids involved in α₁‐β interaction in voltage‐dependent Ca²⁺ channels