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Replacing Leu with Gly (L150G) in Calu1 enables the protein to adopt a structural fold even in the Ca(2+) free form. The fourth (of seven) EF-hand of HsCalu1 nucleates the structural fold of the protein depending on the switch residue (Gly or Leu).
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The Calumenin modulates Sarco/Endoplasmic reticulumCa2+ATPase (SERCA) pump activity without drastically affecting ER-Ca(2+) concentration.
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irradiated tumor cells were observed to significantly up-regulate the expression of calcium-binding proteins CALM1, CALU, and RCN1, suggesting important roles for these mediators in promoting irradiated tumor cell survival during hypoxia
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Calu-15, a novel isoform of Calu with phosphorylation-dependent nuclear localization, has a critical role in promoting filopodia formation and cell migration by upregulating the GDF-15 transcription.
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Results provide direct evidence for the involvement of CALU and LGALS3BP as potential negative regulators in the virus-triggered induction of the typeI interferons.
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Results show that OSBPL5 and CALU were expressed at higher levels in the lung tissues of metastasis-positive cases than that in the metastasis-negative cases suggesting they can promote invasiveness of lung cancer cells.
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CALU polymorphism A29809G affects calumenin availability involving vascular calcification
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Calumenin is characterized as a charged protein exhibiting close similarity with intrinsically disordered proteins and is hypothesized to regulate F508del-CFTR folding by electrostatic effects.
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Calumenin is a new CFTR chaperone.
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Study found the secretion of calu-1/2-EGFP required microtubule integrity, and that calu-1/2-EGFP-containing vesicles were transported by the motor proteins Kif5b and cytoplasmic dynein.
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Quantitative PCR assays for VKORC1, CYP4F2, GGCX and CALU identified two copies in all populations.
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associated with arterial calcification and short-term prognosis of the outcome of patients with non-ST-elevation acute coronary syndrome
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Data show that calumenin in the presence of calcium binds specifically to thrombospondin-1, but closely-related reticulocalbin does not form a similar complex.
