RETRACTED: Molecular structure and target recognition of neuronal calcium sensor proteins
Why is this work in the frame?
A frame that forgets how it found something cannot be audited. These are the routes that admitted this work.
Post-publication record
- Nature
- Retraction
- Reason
- Duplication of/in Article;
- Date
- 5/20/2016 0:00
- Flagged by OpenAlex?
- Yes
Source: Retraction Watch, joined by DOI. OpenAlex records retraction as is_retracted, a boolean over a state space with at least four values, so it cannot express an expression of concern, a correction or a reinstatement — it reports them as false, which reads as “fine”.
Abstract
Neuronal calcium sensor (NCS) proteins, a sub-branch of the EF-hand superfamily, are expressed in the brain and retina where they transduce calcium signals and are genetically linked to degenerative diseases. The amino acid sequences of NCS proteins are highly conserved but their physiological functions are quite distinct. Retinal recoverin and guanylate cyclase activating proteins (GCAPs) both serve as calcium sensors in retinal rod cells, neuronal frequenin (NCS1) modulates synaptic activity and neuronal secretion, K(+) channel interacting proteins (KChIPs) regulate ion channels to control neuronal excitability, and DREAM (KChIP3) is a transcriptional repressor that regulates neuronal gene expression. Here we review the molecular structures of myristoylated forms of NCS1, recoverin, and GCAP1 that all look very different, suggesting that the sequestered myristoyl group helps to refold these highly homologous proteins into very different structures. The molecular structure of NCS target complexes have been solved for recoverin bound to rhodopsin kinase (RK), NCS-1 bound to phosphatidylinositol 4-kinase, and KChIP1 bound to A-type K(+) channels. We propose that N-terminal myristoylation is critical for shaping each NCS family member into a different structure, which upon Ca(2+)-induced extrusion of the myristoyl group exposes a unique set of previously masked residues that interact with a particular physiological target.
Fetched live from OpenAlex and de-inverted. Abstracts are not stored in this database: the inverted indexes are 8.6 GB of the frame’s 9.3 GB of text, and the host has 13 GB free.
The record
- Venue
- Frontiers in Molecular Neuroscience
- Topic
- Retinal Development and Disorders
- Field
- Biochemistry, Genetics and Molecular Biology
- Canadian institutions
- University of TorontoOntario Institute for Cancer Research
- Funders
- National Eye InstituteCanadian Institutes of Health ResearchNational Institutes of Health
- Keywords
- RecoverinMyristoylationEF handCell biologyBiologyCalcium-binding proteinCalciumBiochemistryChemistryGeneRhodopsinPeptide sequenceRetinalPhosphorylation
- Has abstract in OpenAlex
- yes