Reactome | Dimerization of procollagen type VI

Dimerization of procollagen type VI

Stable Identifier

R-HSA-1614460

Type

Reaction [binding]

Species

Homo sapiens

Compartment

endoplasmic reticulum lumen

ReviewStatus

5/5

Locations in the PathwayBrowser

Expand all

General

SBML | | PDF

SVG | | PPTX | SBGN

Click the image above or here to open this reaction in the Pathway Browser
The layout of this reaction may differ from that in the pathway view due to the constraints in pathway layout

Collagen type VI forms dimers and tetramers before secretion (Furthmayr et al. 1983, von der Mark et al. 1984, Engel et al. 1985, Colombatti et al. 1987). The monomers associate in antiparallel with a 30nm axial shift, intertwining 4 or 5 times (Furthmayr et al. 1983). These associate laterally to form tetramers (Furthmayr et al. 1983, von der Mark et al. 1984)The tetramers associate to form microfibrils in a non-covalent manner, presumed to be mediated through A domain interactions (Baldock et al. 2003). Collagen type VI chains are extensively post translationally modifed by the hydroxylation of proline and lysine residues (Myllyharju & Kivirikko 2004) and subsequent glycosylation of hydroxylysine, thought to be essential for tetramer formation and secretion (Sipila et al. 2007).

Literature References

PubMed ID	Title	Journal	Year
6307276	Electron-microscopical approach to a structural model of intima collagen Furthmayr, H, Wiedemann, H, Timpl, R, Odermatt, E, Engel, J	Biochem J	1983
12473679	Structural basis of type VI collagen dimer formation Ball, S, Bella, J, Shuttleworth, A, Kielty, CM	J Biol Chem	2003
3938630	Structure and macromolecular organization of type VI collagen Engel, J, Furthmayr, H, Odermatt, E, von der Mark, H, Aumailley, M, Fleischmajer, R, Timpl, R	Ann N Y Acad Sci	1985