Literature DB >> 26861220

Chemical shift assignments of the C-terminal EF-hand domain of α-actinin-1.

Matthew Turner1, David E Anderson1, Sahana Rajan1, Johannes W Hell2, James B Ames3.   

Abstract

The regulation and localization of the neuronal voltage gated Ca(2+) channel CaV1.2 is important for synaptic plasticity associated with learning and memory. The cytoskeletal protein, α-actinin-1 is known to interact with CaV1.2 and stabilize its localization at the postsynaptic membrane. Here we report both backbone and sidechain NMR assignments for the C-terminal EF-hands (EF3 and EF4) of α-actinin-1 (residues 824-892, called ACTN_EF34) bound to the IQ-motif (residues 1644-1665) from CaV1.2 (BMRB accession no. 25902).

Entities:  

Keywords:  CaV1.2; EF-hand; IQ-motif; Long-term depression; Synaptic plasticity; α-Actinin-1

Mesh:

Substances:

Year:  2016        PMID: 26861220      PMCID: PMC4789133          DOI: 10.1007/s12104-016-9670-2

Source DB:  PubMed          Journal:  Biomol NMR Assign        ISSN: 1874-270X            Impact factor:   0.746


  11 in total

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  1 in total

1.  α-Actinin-1 promotes activity of the L-type Ca2+ channel Cav 1.2.

Authors:  Matthew Turner; David E Anderson; Peter Bartels; Madeline Nieves-Cintron; Andrea M Coleman; Peter B Henderson; Kwun Nok Mimi Man; Pang-Yen Tseng; Vladimir Yarov-Yarovoy; Donald M Bers; Manuel F Navedo; Mary C Horne; James B Ames; Johannes W Hell
Journal:  EMBO J       Date:  2020-01-27       Impact factor: 11.598

  1 in total

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