Reactome | DGC complex binds AGRN and HSPG2

DGC complex binds AGRN and HSPG2

Stable Identifier

R-HSA-9914537

Type

Reaction [binding]

Species

Homo sapiens

Compartment

plasma membrane, extracellular region

ReviewStatus

5/5

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Alpha-dystroglycan (DAG1(30-653)) binds G domain-like sequences in other extracellular matrix molecules such as AGRN (agrin) (Gee et al. 1993; Campanelli et al. 1994; Sugiyama et al. 1994; Yamada et al. 1996; Gesemann et al. 1996) and HSPG2 (perlecan) (Peng et al. 1998; Talts et al. 1999). AGRN is a heparin sulfate basal lamina glycoprotein with roles in the neuromuscular junction (Groffen et al, 1998). HSPG2 is a modular proteoglycan primarily located in the basement membrane of vascularized tissues. It is involved in several developmental processes, both during embryogenesis and in human diseases such as cancer and diabetes (Iozzo et al, 1994). Domain V of the core protein binds alpha-dystroglycan (Talts et al, 1999).
Dag1 knockout mice exhibit severe disruption of basement membranes and embryonic stem cells fail to deposit laminin, suggesting a role for DAG1 in laminin matrix formation (Henry & Campbell 1998). Conditional ablation of DAG1 expression in cultured mammary epithelial cells disrupted laminin-111-induced polarity and beta-casein production, and abolished laminin binding and assembly on the cell surface. Dystroglycan re-expression restored these deficiencies (Weir et al. 2006).

Literature References

PubMed ID	Title	Journal	Year
8205616	A role for dystrophin-associated glycoproteins and utrophin in agrin-induced AChR clustering Campanelli, JT, Roberds, SL, Campbell, KP, Scheller, RH	Cell	1994
7945186	The biology of perlecan: the multifaceted heparan sulphate proteoglycan of basement membranes and pericellular matrices Iozzo, RV, Cohen, IR, Grässel, S, Murdoch, AD	Biochem J	1994
9652404	Primary structure and high expression of human agrin in basement membranes of adult lung and kidney Groffen, AJ, Buskens, CA, van Kuppevelt, TH, Veerkamp, JH, Monnens, LA, van den Heuvel, LP	Eur J Biochem	1998
8627307	Characterization of dystroglycan-laminin interaction in peripheral nerve Yamada, H, Chiba, A, Endo, T, Kobata, A, Anderson, LV, Hori, H, Fukuta-Ohi, H, Kanazawa, I, Campbell, KP, Shimizu, T, Matsumura, K	J. Neurochem.	1996
8325873	Laminin-binding protein 120 from brain is closely related to the dystrophin-associated glycoprotein, dystroglycan, and binds with high affinity to the major heparin binding domain of laminin Gee, SH, Blacher, RW, Douville, PJ, Provost, PR, Yurchenco, PD, Carbonetto, S	J. Biol. Chem.	1993
8607994	Alternative splicing of agrin alters its binding to heparin, dystroglycan, and the putative agrin receptor Gesemann, M, Cavalli, V, Denzer, AJ, Brancaccio, A, Schumacher, B, Ruegg, MA	Neuron	1996
9791728	The relationship between perlecan and dystroglycan and its implication in the formation of the neuromuscular junction Peng, HB, Ali, AA, Daggett, DF, Rauvala, H, Hassell, JR, Smalheiser, NR	Cell Adhes. Commun.	1998
16968749	Dystroglycan loss disrupts polarity and beta-casein induction in mammary epithelial cells by perturbing laminin anchoring Weir, ML, Oppizzi, ML, Henry, MD, Onishi, A, Campbell, KP, Bissell, MJ, Muschler, JL	J. Cell. Sci.	2006
10022829	Binding of the G domains of laminin alpha1 and alpha2 chains and perlecan to heparin, sulfatides, alpha-dystroglycan and several extracellular matrix proteins Talts, JF, Andac, Z, Göhring, W, Brancaccio, A, Timpl, R	EMBO J.	1999
9865703	A role for dystroglycan in basement membrane assembly Henry, MD, Campbell, KP	Cell	1998
8043271	Dystroglycan binds nerve and muscle agrin Sugiyama, J, Bowen, DC, Hall, ZW	Neuron	1994