Disease relevance of CAMLG

• The antiapoptotic proteins K7 and K15 from avian encephalomyelitis virus (AEV) and viral mitochondria inhibitor of apoptosis (vMIA) from cytomegalovirus are capable of binding host-specific apoptosis-modulatory proteins such as Bax, Bcl-2, activated caspase 3, CAML, CIDE-B and HAX [1].

High impact information on CAMLG

• CAML appears to be a new participant in the calcium-signal transduction pathway, implicating cyclophilin B in calcium signalling, even in the absence of cyclosporin [2].
• TACI-induced activation of NF-AT was specifically blocked by a dominant-negative CAML mutant, thus implicating CAML as a signaling intermediate [3].
• The CAML (calcium-modulator and cyclophilin ligand) protein is a coinducer of NF-AT activation when overexpressed in Jurkat T cells [3].
• The defect in these cell lines probably lies between CAML and calcineurin in the T cell activation cascade [4].
• Fractionation of cell extracts on discontinuous sucrose gradients and indirect immunofluorescence indicate that CAML co-localizes with sarcoplasmic/endoplasmic reticulum calcium/ATPase-2 and calreticulin at membrane-bound cytosolic vesicles [5].

Biological context of CAMLG

• The gene for calcium-modulating cyclophilin ligand (CAMLG) is located on human chromosome 5q23 and a syntenic region of mouse chromosome 13 [6].
• The CAMLG gene encodes a novel cyclophilin B-binding protein called calcium-modulating cyclophilin ligand, which appears to be involved in the regulation of calcium signaling in T lymphocytes and other cells [6].
• To study its function in the mouse, we disrupted the CAML gene and found it to be required for early embryonic development, but not for cellular viability [7].
• Mutational analysis showed that K7 interaction with CAML is required for its function in the inhibition of apoptosis [8].
• Similar to CAML, K7 expression significantly enhances the kinetics and amplitudes of the increase in intracellular Ca(2+) concentration on apoptotic stimulus [8].

Anatomical context of CAMLG

• Calcium-modulating cyclophilin ligand (CAML) is a ubiquitous protein that has been implicated in signaling from the cell surface receptor TACI in lymphocytes, although its role and mechanism of action are unknown [7].
• In the present study, we investigated the consequence of CAML overexpression on Ca(2+) signaling using rapid confocal imaging of Fluo3-loaded NIH3T3 fibroblasts [9].

Associations of CAMLG with chemical compounds

• Identification of calcium-modulating cyclophilin ligand (CAML) as transducer of angiotensin II-mediated nuclear factor of activated T cells (NFAT) activation [10].
• From the screening, we found calcium modulating cyclophilin ligand (CAML), a protein involved in Ca(2+) signaling [11].
• Limited trypsin digests indicate that the hydrophilic NH2-terminal domain of CAML is directed toward the cytoplasm [5].
• The human Taci gene (Transmembrane Activator and CAML Interactor) encodes a recently discovered member of the Tumor Necrosis Factor Receptor family [12].

Other interactions of CAMLG

• FGFR1 and CAMLG were more frequently significantly overexpressed in patients with CD56 immunophenoytpe [13].

References