DGC complex binds AGRN and HSPG2

Stable Identifier
R-HSA-9914537
Type
Reaction [binding]
Species
Homo sapiens
Compartment
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

Scheller, RH, Campanelli, JT, Roberds, SL, Campbell, KP

Cell 1994
7945186 The biology of perlecan: the multifaceted heparan sulphate proteoglycan of basement membranes and pericellular matrices

Murdoch, AD, Iozzo, RV, Cohen, IR, Grässel, S

Biochem J 1994
9652404 Primary structure and high expression of human agrin in basement membranes of adult lung and kidney

Monnens, LA, van Kuppevelt, TH, van den Heuvel, LP, Groffen, AJ, Buskens, CA, Veerkamp, JH

Eur J Biochem 1998
8627307 Characterization of dystroglycan-laminin interaction in peripheral nerve

Matsumura, K, Kanazawa, I, Endo, T, Yamada, H, Fukuta-Ohi, H, Anderson, LV, Shimizu, T, Kobata, A, Hori, H, Chiba, A, Campbell, KP

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

Provost, PR, Douville, PJ, Gee, SH, Blacher, RW, Carbonetto, S, Yurchenco, PD

J. Biol. Chem. 1993
8607994 Alternative splicing of agrin alters its binding to heparin, dystroglycan, and the putative agrin receptor

Brancaccio, A, Denzer, AJ, Cavalli, V, Ruegg, MA, Schumacher, B, Gesemann, M

Neuron 1996
9791728 The relationship between perlecan and dystroglycan and its implication in the formation of the neuromuscular junction

Smalheiser, NR, Daggett, DF, Peng, HB, Rauvala, H, Hassell, JR, Ali, AA

Cell Adhes. Commun. 1998
16968749 Dystroglycan loss disrupts polarity and beta-casein induction in mammary epithelial cells by perturbing laminin anchoring

Weir, ML, Onishi, A, Oppizzi, ML, Henry, MD, Muschler, JL, Bissell, MJ, Campbell, KP

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

Brancaccio, A, Timpl, R, Talts, JF, Göhring, W, Andac, Z

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

Hall, ZW, Sugiyama, J, Bowen, DC

Neuron 1994
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