Overview
- Peptide (C)KLEDHEYKPLDPKDIR, corresponding to amino acid residues 669-684 of mouse CHERP (Accession Q8CGZ0). Cytoplasm.
- Mouse brain sections.
- Expression of CHERP in mouse brainImmunohistochemical staining of mouse cortex and hippocampus using Anti-CHERP-ATTO Fluor-594 Antibody (#ACC-330-AR). A. CHERP staining (red) in cortex appears in in cortical neurons (arrows). B. In hippocampus, CHERP staining (red) appears in neurons of pyramidal layer (P) in CA3 region. Nuclei are stained using DAPI (blue).
CHERP (calcium homeostasis endoplasmic reticulum protein) is a ubiquitously expressed integral sarco/endoplasmic reticulum (SR/ER) membrane protein. CHERP protein consist of 916 amino acid in humans and its structure containing a Pro-rich region and a segment of Arg-Ser dipeptide repeats (an RS domain) near the C terminus, and an RNA recognition motifs (RRMs)1-3.
CHERP acts as a regulator of both major families of endoplasmic reticulum Ca2+ channels, inositol 1,4,5-trisphosphate receptors (IP3Rs) and ryanodine receptors (RyRs). CHERP is responsible for the regulation of intracellular Ca2+ mobilization in human cells and is involved in neuroblastoma cell proliferation, apoptosis and tumorigenicity1,2.
CHERP co-localizes with IP3 receptors throughout the cytoplasmic and perinuclear regions in human erythroleukemia cells and in Jurkat cells. CHERP is also detected in the nucleoplasm with prominent accumulation at nuclear speckles1,2. CHERP co-localizes with endogenous ryanodine receptor type 1 (RyR1) in the sarcoplasmic reticulum of rat soleus muscle. Studies of CHERP knockdown reveal decreased intracellular Ca2+ mobilization, cell growth and proliferation2,3.