TY  - GEN
T1  - Mutations in the cell-binding motif of lam-3/laminin α reveal hypercontraction behavior and defective sensitivity to levamisole in Caenorhabditis elegans
AU  - Wang, Lianzijun
AU  - Qiu, Zhongqiang
AU  - Lee, Myeongwoo
DO  - 10.17912/micropub.biology.000485
UR  - http://beta.micropublication.org/journals/biology/micropub-biology-000485/
AB  - Laminin is a heterotrimeric glycoprotein composed of α, β, and γ subunits, one of the significant components in the basement membrane extracellular matrix (ECM). It plays an essential role in tissue organization such as ECM assembly, cell migration, and cell adhesion (Colognato and Yurchenco 2000). In the ECM, laminin interacts with cell surface receptors such as integrins and dystroglycan, linking ECM to actin cytoskeletons in muscle cells (Gawlik et al. 2006; Meinen et al. 2007). Among the laminin subunits, several laminin α chains bind to integrins. There are five α chains in humans. LAMA5 (laminin α5) contains the RGD motifs in its laminin IV type A domain (L4a). In C. elegans, LAM-3/laminin α possesses an RGD motif in the L4a domain, similar to the RGD location in LAMA5 (Figure 1A). Dystroglycan is a non-integrin binding receptor that bridges laminin to the cytoskeleton in skeletal muscle cells. Dystrophin and other transmembrane proteins are collectively identified as the dystrophin-glycoprotein complex that binds to laminins. Deficiencies in dystroglycan complex and laminin are linked to congenital muscular dystrophy (Sciandra et al. 2007; Sciandra et al. 2015). We surveyed ECM proteins and found an RGD (Arg-Gly-Asp) motif in LAM-3/laminin α (amino acid numbers 1462, 1463, and 1464). The RGD motif was edited to RGE or deleted to study the function of the motif.
PY  - 2021
JO  - microPublication Biology
ER  -