Редактирование: ANKRD1 (раздел)

==Publications==

{{medline-entry
|title=[[ANKRD1]] specifically binds [[CASQ2]] in heart extracts and both proteins are co-enriched in piglet cardiac Purkinje cells.
|pubmed-url=https://pubmed.ncbi.nlm.nih.gov/15698842
|abstract=It has been suggested that the cardiac ankyrin repeat domain 1 protein ([[ANKRD1]]), also known as CARP, can play a pathophysiological role in the contractile responsiveness of myocardium. Here, we study the potential functional roles of [[ANKRD1]] by searching for endogenous cardiac proteins that interact preferentially with [[ANKRD1]] in the heart-tissue extract from neonatal piglets, using non-biased pull-down approaches. These approaches identified, for the first time, a selective interaction between [[ANKRD1]] and endogenous cardiac calsequestrin-2 ([[CASQ2]]) that is important for Ca2  release and excitation-contraction coupling. Blot-overlay and co-immunoprecipitation assays provided further confirmation of the direct and specific interaction between the two proteins. Mapping of the peptides involved in the interaction revealed five non-overlapping binding sequences for [[CASQ2]] on [[ANKRD1]], as well as, three binding peptides for [[ANKRD1]] in [[CASQ2]]. For the first time, we show by immunohistochemistry that endogenous [[ANKRD1]] and [[CASQ2]] are co-enriched in piglet cardiac Purkinje cells. Collectively, the results provide the first sing of a possible functional interaction between [[ANKRD1]] and [[CASQ2]] and suggest a potentially novel role for both proteins in cardiac Purkinje fibers.
|mesh-terms=* Aging
* Amino Acid Sequence
* Animals
* Binding Sites
* Calcium
* Calsequestrin
* Cell Extracts
* Dogs
* Heart
* Humans
* Immunohistochemistry
* Molecular Sequence Data
* Myocardium
* Nuclear Proteins
* Protein Binding
* Purkinje Cells
* Repressor Proteins
* Substrate Specificity
* Swine
* Tissue Extracts

|full-text-url=https://sci-hub.do/10.1016/j.yjmcc.2004.11.034
}}