What does Dystroglycan do?
Dystroglycan is an extracellular matrix receptor involved in adhesion. This protein plays an important role in wound repair of epithelium, and thus may play a role in the progressive impairment of wound repair capacity that occurs in BPD.
What is β Dystroglycan?
β-Dystroglycan is a single-pass transmembrane protein with a largely unstructured amino-terminal extracellular domain that binds to the carboxy-terminal globular domain of α-dystroglycan (Di et al., 1999; Boffi et al., 2001) and a 121-residue carboxy-terminal cytoplasmic domain that binds directly to the WW, EF, and ZZ …
What is alpha Dystroglycan?
α-dystroglycan (α-DG) is an extracellular membrane-associated protein that binds to a variety of extracellular matrix proteins including laminin-α2 [19], while β-dystroglycan (β-DG) is a transmembrane protein that binds strongly to α-DG via its extracellular domain and to dystrophin (and utrophin) via its intracellular …
Where is Dystroglycan?
α-Dystroglycan is a peripheral membrane component of the dystrophin–glycoprotein complex (DGC) found in muscle, nerve, heart, and brain. This protein binds to merosin in extracellular matrix bridging it to the cytoskeleton molecules that include dystrophin and actin.
Where is Pikachurin found?
Pikachurin is the most recently identified dystroglycan ligand protein and is localized in the synaptic cleft in the photoreceptor ribbon synapse.
Where is utrophin found?
neuromuscular junction
In normal skeletal muscle, utrophin is found at the neuromuscular junction (NMJ) whereas dystrophin predominates at the sarcolemma. However, during development, and in some myopathies including DMD, utrophin is also found at the sarcolemma.
What is the dystroglycan complex?
The dystroglycan complex contains the transmembrane protein β-dystroglycan and its interacting extracellular mucin-like protein α-dystroglycan. In skeletal muscle fibers, the dystroglycan complex plays an important structural role by linking the cytoskeletal protein dystrophin to laminin in the extracellular matrix.
What is the cell that looks like a cross?
Thus, laminin-511 contains α5, β1, and γ1 chains. Fourteen other chain combinations have been identified in vivo….Laminin domains.
| Laminin EGF-like (Domains III and V) | |
|---|---|
| Pfam | PF00053 |
| Pfam clan | CL0001 |
| InterPro | IPR002049 |
| PROSITE | PDOC00021 |
What is the function of Pikachurin?
Pikachurin is a dystroglycan-interacting protein which has an essential role in the precise interactions between the photoreceptor ribbon synapse and the bipolar dendrites.
Is Pikachu a mouse?
Pikachu is a yellow mouse-like Pokémon with powerful electrical abilities. Pikachu’s design was conceived by Atsuko Nishida and finalized by Ken Sugimori.
How can I increase my utrophin?
Upregulation of utrophin can be achieved by protein delivery or by upregulating the native endogenous utrophin promoter. Increasing native utrophin levels by 2–3-fold may be sufficient to improve muscle degeneration in DMD since muscles showing this modest level of overexpression are protected.
What is the role of utrophin?
In mature human muscle, utrophin is found mostly at the neuromuscular junction where it is thought to physically stabilize and protect this specialized synapse. Utrophin has a secondary role during muscle development when it is expressed highly and is found along the sarcolemma [155].
What kind of gene is DAG1 dystroglycan 1?
DAG1 dystroglycan 1 [ (human)] Gene ID: 1605, updated on 2-Dec-2016. This gene encodes dystroglycan, a central component of dystrophin-glycoprotein complex that links the extracellular matrix and the cytoskeleton in the skeletal muscle.
What are the effects of mutations in DAG1?
Novel mutations in DAG1 are associated with asymptomatic hyperCKemia with hypoglycosylation of alpha-dystroglycan. Reduction of alpha-dystroglycan expression is correlated with glioma.
How does DAG1 interact with the Hippo pathway?
In mice, Morikawa et al. (2017) demonstrated that Dag1 directly binds to the Hippo pathway effector Yap ( 606608) to inhibit cardiomyocyte proliferation. The Yap-Dag1 interaction was enhanced by Hippo-induced Yap phosphorylation, revealing a connection between Hippo pathway function and the dystrophin-glycoprotein complex.