Dystroglycan: a multifunctional adaptor protein

Higginson, J.R.; Winder, Steve J.

doi:10.1042/bst20051254

Cited by 14 publications

(4 citation statements)

References 14 publications

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“…ILK is essential for the force-transducing function of β1 integrins that bind both LN-511 and LN-332 with high affinity 55 . Interestingly, dystroglycans that are ECM-assembling receptors linked to the actin cytoskeleton, do not bind efficiently to LN-332 but have high affinity to LN-511 (refs 56 , 57 ). Dystroglycans do not require ILK for their function and could compensate for the loss of β1-integrin-ILK function selectively in LN-511 deposition, leading to an imbalance in the ratio of LN-511 and LN-332.…”

Section: Discussionmentioning

confidence: 99%

Integrin-linked kinase regulates the niche of quiescent epidermal stem cells

et al. 2015

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Stem cells reside in specialized niches that are critical for their function. Quiescent hair follicle stem cells (HFSCs) are confined within the bulge niche, but how the molecular composition of the niche regulates stem cell behaviour is poorly understood. Here we show that integrin-linked kinase (ILK) is a key regulator of the bulge extracellular matrix microenvironment, thereby governing the activation and maintenance of HFSCs. ILK mediates deposition of inverse laminin (LN)-332 and LN-511 gradients within the basement membrane (BM) wrapping the hair follicles. The precise BM composition tunes activities of Wnt and transforming growth factor-β pathways and subsequently regulates HFSC activation. Notably, reconstituting an optimal LN microenvironment restores the altered signalling in ILK-deficient cells. Aberrant stem cell activation in ILK-deficient epidermis leads to increased replicative stress, predisposing the tissue to carcinogenesis. Overall, our findings uncover a critical role for the BM niche in regulating stem cell activation and thereby skin homeostasis.

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Section: Discussionmentioning

confidence: 99%

Integrin-linked kinase regulates the niche of quiescent epidermal stem cells

et al. 2015

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“…β-DG is a key protein with versatile functions [ 64 ], that participates in cell signaling during cell polarity or cancer progression [ 65 , 66 ]. Its signaling functions are associated to the presence of over 40 protein interactive domains, and 19 functional motifs, present at the β-DG C-terminal region rich in proline residues [ 67 ].…”

Section: Discussionmentioning

confidence: 99%

Novel Nuclear Protein Complexes of Dystrophin 71 Isoforms in Rat Cultured Hippocampal GABAergic and Glutamatergic Neurons

et al. 2015

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The precise functional role of the dystrophin 71 in neurons is still elusive. Previously, we reported that dystrophin 71d and dystrophin 71f are present in nuclei from cultured neurons. In the present work, we performed a detailed analysis of the intranuclear distribution of dystrophin 71 isoforms (Dp71d and Dp71f), during the temporal course of 7-day postnatal rats hippocampal neurons culture for 1h, 2, 4, 10, 15 and 21 days in vitro (DIV). By immunofluorescence assays, we detected the highest level of nuclear expression of both dystrophin Dp71 isoforms at 10 DIV, during the temporal course of primary culture. Dp71d and Dp71f were detected mainly in bipolar GABAergic (≥60%) and multipolar Glutamatergic (≤40%) neurons, respectively. We also characterized the existence of two nuclear dystrophin-associated protein complexes (DAPC): dystrophin 71d or dystrophin 71f bound to β-dystroglycan, α1-, β-, α2-dystrobrevins, α-syntrophin, and syntrophin-associated protein nNOS (Dp71d-DAPC or Dp71f-DAPC, respectively), in the hippocampal neurons. Furthermore, both complexes were localized in interchromatin granule cluster structures (nuclear speckles) of neuronal nucleoskeleton preparations. The present study evinces that each Dp71’s complexes differ slightly in dystrobrevins composition. The results demonstrated that Dp71d-DAPC was mainly localized in bipolar GABAergic and Dp71f-DAPC in multipolar Glutamatergic hippocampal neurons. Taken together, our results show that dystrophin 71d, dystrophin 71f and DAP integrate protein complexes, and both complexes were associated to nuclear speckles structures.

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“…Indications for a putative role of actin in astrocytes are indirect, reported from loss-of-function studies and cell culture experiments. Astrocyte endfeet have enriched protein complexes composed of the transmembrane protein dystroglycan and its associated ligands syntrophin and dystrophin, and in other cell types this complex bridges the actin cytoskeleton with laminins in the extracellular matrix (Higginson and Winder, 2005 ). Moreover, the defined localization of potassium channels and aquaporin-4 in the plasma membrane of endfeet partially depends on tethered dystroglycan protein complexes.…”

Section: Stars With Sensitive Feetmentioning

confidence: 99%

Important Shapeshifter: Mechanisms Allowing Astrocytes to Respond to the Changing Nervous System During Development, Injury and Disease

Schiweck

Eickholt

Murk

2018

Front. Cell. Neurosci.

174

188

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Astrocytes are the most prevalent glial cells in the brain. Historically considered as “merely supporting” neurons, recent research has shown that astrocytes actively participate in a large variety of central nervous system (CNS) functions including synaptogenesis, neuronal transmission and synaptic plasticity. During disease and injury, astrocytes efficiently protect neurons by various means, notably by sealing them off from neurotoxic factors and repairing the blood-brain barrier. Their ramified morphology allows them to perform diverse tasks by interacting with synapses, blood vessels and other glial cells. In this review article, we provide an overview of how astrocytes acquire their complex morphology during development. We then move from the developing to the mature brain, and review current research on perisynaptic astrocytic processes, with a particular focus on how astrocytes engage synapses and modulate their formation and activity. Comprehensive changes have been reported in astrocyte cell shape in many CNS pathologies. Factors influencing these morphological changes are summarized in the context of brain pathologies, such as traumatic injury and degenerative conditions. We provide insight into the molecular, cellular and cytoskeletal machinery behind these shape changes which drive the dynamic remodeling in astrocyte morphology during injury and the development of pathologies.

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Dystroglycan: a multifunctional adaptor protein

Cited by 14 publications

References 14 publications

Integrin-linked kinase regulates the niche of quiescent epidermal stem cells

Integrin-linked kinase regulates the niche of quiescent epidermal stem cells

Novel Nuclear Protein Complexes of Dystrophin 71 Isoforms in Rat Cultured Hippocampal GABAergic and Glutamatergic Neurons

Important Shapeshifter: Mechanisms Allowing Astrocytes to Respond to the Changing Nervous System During Development, Injury and Disease

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