Integrin on developing and adult skeletal muscle

Bozyczko, Donna; Decker, C; Muschler, John; Horwitz, Alan F.

doi:10.1016/0014-4827(89)90419-9

Cited by 118 publications

(70 citation statements)

References 44 publications

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“…Immunofluorescence analysis showed that Melusin is localized in rows flanking the Z line containing ␣-actinin. Similar pattern has been described for vinculin (37) and ␤ 1 integrin (12,13,10) and is thought to correspond to sites of lateral interaction of actin with the plasma membrane known as costameres (37,38). This pattern of localization suggests that Melusin is a component of the actin-integrin junctional complex in muscle.…”

Section: Fig 4 Melusin Is Enriched At Costameres Panels In Left Cosupporting

confidence: 68%

“…At myotendinous junctions, actomyosin filaments are anchored end-on to the plasma membrane, whereas at costamers they are joined laterally. Integrins are selectively enriched both in myotendinous junctions and costamers (10,12,13), suggesting an important role of these receptors in connecting the cytoskeleton to the extracellular matrix in muscles. Direct evidence of the role of integrins in muscle function and in actin organization also comes from gene knockout experiments.…”

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confidence: 99%

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Melusin Is a New Muscle-specific Interactor for β1Integrin Cytoplasmic Domain

Brancaccio

Guazzone

Menini

et al. 1999

Journal of Biological Chemistry

102

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Section: Fig 4 Melusin Is Enriched At Costameres Panels In Left Cosupporting

confidence: 68%

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confidence: 99%

Melusin Is a New Muscle-specific Interactor for β1Integrin Cytoplasmic Domain

Brancaccio

Guazzone

Menini

et al. 1999

Journal of Biological Chemistry

102

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“…Several observations in cultured vertebrate cells indicate that the association of integrins with Z-bands may be a late step in sarcomere formation (Bozyczko et al, 1989;Hilenski et al, 1991) or may not occur at all (Bozyczko et al, 1989;Lu et al, 1992). This would suggest that linkage of a vertebrate cytoskeleton with the extracellular matrix through integrins at Z-bands may be a more stabilizing than initiating event of myogenesis.…”

Section: Discussionmentioning

confidence: 99%

Differentiation, extracellular matrix synthesis, and integrin assembly by Drosophila embryo cells cultured on vitronectin and laminin substrates

Gullberg¹,

Fessler²,

Fessler³

1994

Developmental Dynamics

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ABSTRACTwas unnecessary for myotube formation on laminin, it was required for the subsequent change to a sarcomeric cytoarchitecture. The differentiating primary cultures synthesized integrins and assembled them into detergent-insoluble, cytoskeleton-associated complexes. Collagen IV, laminin, glutactin, papilin, and other extracellular matrix proteins were made primarily by hemocytes and were secreted into the medium. Further differentiation within the cultures was influenced by secreted components and by later addition of vitronectin or bovine serum. Comparison of the differentiation of various cell types on the two substrates showed that vitronectin provided a selective advantage for the differentiation of myocytes, with enrichment over epithelia, epidermal cells, and neurites. 0 1994 Wiley-Liss, Inc.

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“…The subsarcolemma density of this junction is the site of insertion of the actin filaments that emanate from the terminal Z-disc of the myofibrils [231, 2401. Junctional components (Table 1) include vinculin and talin on the cytoplasmic face [26,232,2331 and transmembrane integrins [26, 2211 that link to basement-membrane-matrix molecules including laminin and heparin sulphate proteoglycans [50,221]. Interestingly, a-actinin appears to be excluded from this junction [231].…”

Section: The Rnyotendinous Junctionmentioning

confidence: 99%

The cytoskeletal lattice of muscle cells

Small

Fürst

Thornell

1992

European Journal of Biochemistry

141

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By modulating the level of structural organization of two primary components, actin and myosin, nature has devised a wide range of actin-based motile systems. At one extreme is the cross-striated muscle cell with its highly ordered and stable arrangement of filaments, specialised for rapid contractions. And at the other are non-muscle cells, like fibroblasts and amoebae, whose dynamic protrusive movements depend on the continual growth and breakdown of less organised actin filament arrays coupled, in some way, with the shearing of monomeric, tailless myosin molecules.Left to their own devices, in vitro, actin and myosin filaments can form contractile threads [268] but these are poorly organized and inefficient. Order in contractile assemblies must therefore be brought about by other components, accessory molecules, whose function is to link filaments with each other and with the cell membrane. In order to characterise such accessory molecules and gain insight into assembly principles, efforts have been mainly concentrated on vertebrate skeletal muscle. This system has been favoured, first, because it readily facilitates a combined biochemical and microscopic approach and, second, because early data (reviewed in [261 I) had already pointed to the existence in the sarcomere of structural material distinct from the contractile elements. Results accumulated over the last decade or so from skeletal muscle, together with complementary data from other systems, has now led to the recognition of a complex structural lattice in muscle cells; included in this lattice is an organised membrane skeleton whose components may play roles in maintaining sarcomere integrity. The purpose ofthis review is to survey recent advances in our understanding of the organisation and function of this structural lattice. The starting point is skeletal muscle but we shall also analyse cardiac and smooth muscle as well as other muscle types for which relevant information is available. CROSS-STRIATED MUSCLEIt is notable that the first indications of the existence of a structural lattice in striated muscle came in parallel with the discovery of the actin-and myosin-based sliding filament Correspondence to J. V. Small, Institute of Molecular Biology, Austrian Academy of Sciences, Billrothstrasse 1 1, A-5020 Salzburg, Austria mechanism of contraction. Thus, Huxley and Hanson [94] established that the total extraction of myosin from myofibrils yielded 'ghost myofibrils' that were both continuous and extensible. The results of subsequent work (reviewed in [139, 2611) have shown that this continuity is maintained by an endosarcomeric lattice (Fig. 1) containing two extended, highmolecular-mass proteins, titin and nebulin. Homologues of vertebrate muscle titin (also called connectin) [140] found in invertebrates, have been referred to as twitchin [16] and projectin [191]. Included in the sarcomeric lattice are the Z and M discs ('Zwischenscheibe' and 'Mittellinie') that serve as structural integrators of the myofilaments and the longitudinal latti...

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Integrin on developing and adult skeletal muscle

Cited by 118 publications

References 44 publications

Melusin Is a New Muscle-specific Interactor for β1Integrin Cytoplasmic Domain

Melusin Is a New Muscle-specific Interactor for β1Integrin Cytoplasmic Domain

Differentiation, extracellular matrix synthesis, and integrin assembly by Drosophila embryo cells cultured on vitronectin and laminin substrates

The cytoskeletal lattice of muscle cells

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