Disease relevance of CETN2

• Centrosome protein centrin 2/caltractin 1 is part of the xeroderma pigmentosum group C complex that initiates global genome nucleotide excision repair [1].
• The normal response after CALT (cold/warm, monaurally performed) consists of transient ataxia and body sway towards the side of the nystagmic slow phase induced by a similar CALT [2].

High impact information on CETN2

• Binding experiments with a series of truncated XPC proteins allowed the centrin 2 binding domain to be mapped to a presumed alpha-helical region near the C terminus, and three amino acid substitutions in this domain abrogated interaction with centrin 2 [3].
• Centrin 2 stimulates nucleotide excision repair by interacting with xeroderma pigmentosum group C protein [3].
• To determine the structure of human centrin-2 and to develop an understanding of molecular interactions between centrin and xeroderma pigmentosum group C protein, we characterized the crystal structure of calcium-loaded full-length centrin-2 complexed with a xeroderma pigmentosum group C peptide [4].
• Human centrin-2 plays a key role in centrosome function and stimulates nucleotide excision repair by binding to the xeroderma pigmentosum group C protein [4].
• Human centrin 2 (HsCen2), a member of the EF-hand superfamily of Ca2+-binding proteins, is commonly associated with centrosome-related structures [5].

Biological context of CETN2

• Thus, those findings suggest that the XPC-CEN2 interaction may reflect coupling of cell division and NER [1].
• The main molecular partner in the centrosome is a small, calcium-binding EF-hand protein, the human centrin 2 [6].
• The target binding site is localized within the C-terminal domain of human centrin 2 [6].
• RESULTS: Here, using RNA interference, we demonstrate that "knockdown" of centrin-2, a protein of centrioles, results in failure of centriole duplication during the cell cycle in HeLa cells [7].
• While the gene for Cetn 1 contains no introns and appears to be derived from Cetn 2 by retroposition, a gene product for Cetn 1 is expressed [8].

Anatomical context of CETN2

• CEN2 has been shown to play an important role in centrosome duplication [1].
• Centrin-2 is required for centriole duplication in mammalian cells [7].
• We found only one example of organised conjunctival lymphoid tissue in our study and suggest that the presence of CALT in humans is not universal [9].

Associations of CETN2 with chemical compounds

• The two standard peptides bind human centrin 2 and its isolated C-terminal domain with high affinity ( approximately 10(7) m(-1)) by an enthalpy-driven mechanism, with a moderate Ca(2+) dependence [6].

Physical interactions of CETN2

• Flexibility and plasticity of human centrin 2 binding to the xeroderma pigmentosum group C protein (XPC) from nuclear excision repair [10].

Other interactions of CETN2

• Human centrin 2 is a component of the nucleotide excision repair system, as a subunit of the heterotrimer including xeroderma pigmentosum group C protein (XPC) and hHR23B [10].

Analytical, diagnostic and therapeutic context of CETN2

• Assignment of the human caltractin gene (CALT) to Xq28 by fluorescence in situ hybridization [11].
• Crystallization and preliminary X-ray diffraction data of the complex between human centrin 2 and a peptide from the protein XPC [12].
• RT-PCR experiments show that the expression of the three human centrin genes increases during cell differentiation, and that only centrin 2 and 3 are expressed during cell proliferation [13].
• This paper deals with the abnormal responsiveness of the paradoxical stabilizing type (SR) occurring after caloric tests (CALT) performed on a passive force platform [2].

References