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1-3 of 3
Ulrich Müller
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Journal Articles
Hiroshi Nishimune, Gregorio Valdez, George Jarad, Casey L. Moulson, Ulrich Müller, Jeffrey H. Miner, Joshua R. Sanes
Journal:
Journal of Cell Biology
Journal of Cell Biology (2008) 182 (6): 1201–1215.
Published: 15 September 2008
Abstract
A prominent feature of synaptic maturation at the neuromuscular junction (NMJ) is the topological transformation of the acetylcholine receptor (AChR)-rich postsynaptic membrane from an ovoid plaque into a complex array of branches. We show here that laminins play an autocrine role in promoting this transformation. Laminins containing the α4, α5, and β2 subunits are synthesized by muscle fibers and concentrated in the small portion of the basal lamina that passes through the synaptic cleft at the NMJ. Topological maturation of AChR clusters was delayed in targeted mutant mice lacking laminin α5 and arrested in mutants lacking both α4 and α5. Analysis of chimeric laminins in vivo and of mutant myotubes cultured aneurally demonstrated that the laminins act directly on muscle cells to promote postsynaptic maturation. Immunohistochemical studies in vivo and in vitro along with analysis of targeted mutants provide evidence that laminin-dependent aggregation of dystroglycan in the postsynaptic membrane is a key step in synaptic maturation. Another synaptically concentrated laminin receptor, Bcam, is dispensable. Together with previous studies implicating laminins as organizers of presynaptic differentiation, these results show that laminins coordinate post- with presynaptic maturation.
Includes: Multimedia, Supplementary data
Journal Articles
Hao-Ven Wang, Ling-Wei Chang, Klara Brixius, Sara A. Wickström, Eloi Montanez, Ingo Thievessen, Martin Schwander, Ulrich Müller, Wilhelm Bloch, Ulrike Mayer, Reinhard Fässler
Journal:
Journal of Cell Biology
Journal of Cell Biology (2008) 180 (5): 1037–1049.
Published: 10 March 2008
Abstract
Skeletal muscle expresses high levels of integrin-linked kinase (ILK), predominantly at myotendinous junctions (MTJs) and costameres. ILK binds the cytoplasmic domain of β1 integrin and mediates phosphorylation of protein kinase B (PKB)/Akt, which in turn plays a central role during skeletal muscle regeneration. We show that mice with a skeletal muscle–restricted deletion of ILK develop a mild progressive muscular dystrophy mainly restricted to the MTJs with detachment of basement membranes and accumulation of extracellular matrix. Endurance exercise training enhances the defects at MTJs, leads to disturbed subsarcolemmal myofiber architecture, and abrogates phosphorylation of Ser473 as well as phosphorylation of Thr308 of PKB/Akt. The reduction in PKB/Akt activation is accompanied by an impaired insulin-like growth factor 1 receptor (IGF-1R) activation. Coimmunoprecipitation experiments reveal that the β1 integrin subunit is associated with the IGF-1R in muscle cells. Our data identify the β1 integrin–ILK complex as an important component of IGF-1R/insulin receptor substrate signaling to PKB/Akt during mechanical stress in skeletal muscle.
Includes: Supplementary data
Journal Articles
The von Hippel-Lindau tumor suppressor protein controls ciliogenesis by orienting microtubule growth
Bernhard Schermer, Cristina Ghenoiu, Malte Bartram, Roman Ulrich Müller, Fruzsina Kotsis, Martin Höhne, Wolfgang Kühn, Manuela Rapka, Roland Nitschke, Hanswalter Zentgraf, Manfred Fliegauf, Heymut Omran, Gerd Walz, Thomas Benzing
Journal:
Journal of Cell Biology
Journal of Cell Biology (2006) 175 (4): 547–554.
Published: 13 November 2006
Abstract
Cilia are specialized organelles that play an important role in several biological processes, including mechanosensation, photoperception, and osmosignaling. Mutations in proteins localized to cilia have been implicated in a growing number of human diseases. In this study, we demonstrate that the von Hippel-Lindau (VHL) protein (pVHL) is a ciliary protein that controls ciliogenesis in kidney cells. Knockdown of pVHL impeded the formation of cilia in mouse inner medullary collecting duct 3 kidney cells, whereas the expression of pVHL in VHL-negative renal cancer cells rescued the ciliogenesis defect. Using green fluorescent protein–tagged end-binding protein 1 to label microtubule plus ends, we found that pVHL does not affect the microtubule growth rate but is needed to orient the growth of microtubules toward the cell periphery, a prerequisite for the formation of cilia. Furthermore, pVHL interacts with the Par3–Par6–atypical PKC complex, suggesting a mechanism for linking polarity pathways to microtubule capture and ciliogenesis.
Includes: Supplementary data