CRYGC explained

Crystallin, gamma C, also known as CRYGC, is a protein which in humans is encoded by the CRYGC gene.[1] [2]

Function

Crystallins are separated into two classes: taxon-specific, or enzyme, and ubiquitous. The latter class constitutes the major proteins of vertebrate eye lens and maintains the transparency and refractive index of the lens. Since lens central fiber cells lose their nuclei during development, these crystallins are made and then retained throughout life, making them extremely stable proteins. Mammalian lens crystallins are divided into alpha, beta, and gamma families; beta and gamma crystallins are also considered as a superfamily. Alpha and beta families are further divided into acidic and basic groups. Seven protein regions exist in crystallins: four homologous motifs, a connecting peptide, and N- and C-terminal extensions. Gamma-crystallins are a homogeneous group of highly symmetrical, monomeric proteins typically lacking connecting peptides and terminal extensions. They are differentially regulated after early development. Four gamma-crystallin genes (gamma-A through gamma-D) and three pseudogenes (gamma-E, gamma-F, gamma-G) are organized in a genomic segment as a gene cluster. Whether due to aging or mutations in specific genes, gamma-crystallins have been involved in cataract formation.

Interactions

CRYGC has been shown to interact with CRYBB2,[3] CRYAA[3] and CRYAB.[3]

Further reading

Notes and References

  1. den Dunnen JT, Moormann RJ, Cremers FP, Schoenmakers JG . Two human gamma-crystallin genes are linked and riddled with Alu-repeats . Gene . 38 . 1–3 . 197–204 . 1985 . 4065573 . 10.1016/0378-1119(85)90218-5 .
  2. Web site: Entrez Gene: CRYGC crystallin, gamma C.
  3. Fu L, Liang JJ . Detection of protein-protein interactions among lens crystallins in a mammalian two-hybrid system assay . The Journal of Biological Chemistry . 277 . 6 . 4255–60 . February 2002 . 11700327 . 10.1074/jbc.M110027200 . free .