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CALML5 interacts with SFN in suprabasal epidermis, cocontrols 13% of late differentiation genes, and modulates interaction of SFN to some of its binding partners.
CLSP is increased in the upper epidermis in exacerbated atopic dermatitis as compared to non-exacerbated atopic dermatitis and normal skin, revealing a role in re-establishing the epidermal barrier
Ubiquitination of CALML5 in the nucleus is involved in the carcinogenesis of breast cancer in premenopausal women.
CLSP is a physiological heterotrimeric humanin receptor agonist.
An investigation of the cation-binding properties of CLSP and the ensuing conformational changes finds that, with its high- and low-affinity Ca+2+-binding sites and a pronounced effect of Mg2+, CLSP is more similar to troponin C than to calmodulin.
abnormal elevated levels of CLSP, characteristic of psoriatic epidermis, were probably not due to an overexpression of the protein, but most likely the result of its non-degradation
The structure and dynamics of human calmodulin-like skin protein (CLSP) have been characterized by NMR spectroscopy.
Phylogenetic analysis suggests that AtCML4 and AtCML5 are closely related paralogues originating from a duplication event within the Brassicaceae family. Together the results show that CML4/5-like proteins represent a flowering plant-specific subfamily of CMLs with a potential function in vesicle transport within the plant endomembrane system.
This gene encodes a novel calcium binding protein expressed in the epidermis and related to the calmodulin family of calcium binding proteins. Functional studies with recombinant protein demonstrate it does bind calcium and undergoes a conformational change when it does so. Abundant expression is detected only in reconstructed epidermis and is restricted to differentiating keratinocytes. In addition, it can associate with transglutaminase 3, shown to be a key enzyme in the terminal differentiation of keratinocytes.
, calmodulin-like protein 5
, calmodulin-like skin protein