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  • Title: Sc65-Null Mice Provide Evidence for a Novel Endoplasmic Reticulum Complex Regulating Collagen Lysyl Hydroxylation.
    Author: Heard ME, Besio R, Weis M, Rai J, Hudson DM, Dimori M, Zimmerman SM, Kamykowski JA, Hogue WR, Swain FL, Burdine MS, Mackintosh SG, Tackett AJ, Suva LJ, Eyre DR, Morello R.
    Journal: PLoS Genet; 2016 Apr; 12(4):e1006002. PubMed ID: 27119146.
    Abstract:
    Collagen is a major component of the extracellular matrix and its integrity is essential for connective tissue and organ function. The importance of proteins involved in intracellular collagen post-translational modification, folding and transport was recently highlighted from studies on recessive forms of osteogenesis imperfecta (OI). Here we describe the critical role of SC65 (Synaptonemal Complex 65, P3H4), a leprecan-family member, as part of an endoplasmic reticulum (ER) complex with prolyl 3-hydroxylase 3. This complex affects the activity of lysyl-hydroxylase 1 potentially through interactions with the enzyme and/or cyclophilin B. Loss of Sc65 in the mouse results in instability of this complex, altered collagen lysine hydroxylation and cross-linking leading to connective tissue defects that include low bone mass and skin fragility. This is the first indication of a prolyl-hydroxylase complex in the ER controlling lysyl-hydroxylase activity during collagen synthesis.
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