Works (3)
Updated: June 12th, 2023 23:52
2002 journal article
Alternative splicing of a beta(4) subunit proline-rich motif regulates voltage-dependent gating and toxin block of Ca(v)2.1 Ca2+ channels
Journal of Neuroscience, 22(21), 9331–9339.
MeSH headings : Alternative Splicing / physiology; Amino Acid Motifs / physiology; Animals; Brain / metabolism; Calcium Channel Blockers / pharmacology; Calcium Channels, N-Type / drug effects; Calcium Channels, N-Type / genetics; Calcium Channels, N-Type / metabolism; Humans; Ion Channel Gating / drug effects; Ion Channel Gating / physiology; Membrane Potentials / physiology; Models, Molecular; Molecular Sequence Data; Mutagenesis, Site-Directed; Nerve Tissue Proteins / genetics; Oocytes / metabolism; Organ Specificity; Patch-Clamp Techniques; Protein Structure, Tertiary / physiology; Protein Subunits / drug effects; Protein Subunits / genetics; Protein Subunits / metabolism; RNA, Messenger / metabolism; Sequence Deletion; Sequence Homology, Amino Acid; Spinal Cord / metabolism; Structure-Activity Relationship; Xenopus laevis; omega-Conotoxins / pharmacology
TL;DR:
The models reveal that alternative splicing of the β4 N terminus results in dramatic differences in surface charge distribution and localize the proline-rich motif of β4b to an extended arm structure that flanks what would be the equivalent of a highly modified PSD-95 carboxylate binding loop.
(via Semantic Scholar)
Source: NC State University Libraries
Added: August 6, 2018
2002 journal article
Alternative splicing of the beta(4) subunit has alpha(1) subunit subtype-specific effects on Ca2+ channel gating
Journal of Neuroscience, 22(5), 1573–1582.
Source: NC State University Libraries
Added: August 6, 2018
2000 journal article
C-terminal alternative splicing changes the gating properties of a human spinal cord calcium channel alpha 1A subunit
Journal of Neuroscience, 20(20), 7564–7570.
MeSH headings : Alternative Splicing; Amino Acid Substitution; Animals; Calcium Channels / genetics; Calcium Channels / metabolism; Cells, Cultured; Cerebellum / metabolism; Exons; Gene Expression; Humans; Ion Channel Gating / genetics; Membrane Potentials / physiology; Microinjections; Molecular Sequence Data; Nerve Tissue Proteins / genetics; Nerve Tissue Proteins / metabolism; Oocytes / metabolism; Patch-Clamp Techniques; Protein Isoforms / genetics; Protein Isoforms / metabolism; Recombinant Fusion Proteins / genetics; Recombinant Fusion Proteins / metabolism; Spinal Cord / metabolism; Xenopus
TL;DR:
It is demonstrated that C-terminal structural changes alone can influence the way in which α1A subunits respond to a depolarizing stimulus and add to the developing picture of the C terminus as a critical domain in the regulation of Ca2+ channel function.
(via Semantic Scholar)
open access via www.jneurosci.org (publisher PDF)
Source: NC State University Libraries
Added: August 6, 2018
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