Properties of the Novel Intermediate Filament Protein Synemin and Its Identification in Mammalian Muscle

Bilak, Stephan R.; Sernett, Suzanne W.; Bilak, Masako M.; Bellin, Robert M.; Stromer, Marvin H.; Huiatt, Ted W.; Robson, Richard M.

doi:10.1006/abbi.1998.0702

Cited by 83 publications

(77 citation statements)

References 61 publications

Supporting

Mentioning

Contrasting

Unclassified

Order By: Relevance

“…By contrast, in Gfap -/-astrocytes, synemin protein and mRNA levels, as well as synemin incorporation into vimentin IFs, were unaltered. Biochemical assays with purified proteins suggested that synemin interacts with copolymerize with vimentin (Bellin et al, 1999;Bilak et al, 1998;Marvin et al, 1998;Sandoval, 1983;Steinert et al, 1999;Titeux et al, 2001), resembling in this respect the type IV IF protein nestin .…”

Section: Vimmentioning

confidence: 99%

“…They are also highly homologous with the tail and rod domains of desmin, the muscle-specific type III IF protein that coexists with synemin in muscle cells during development and in adulthood (Price and Lazarides, 1993;Bilak et al, 1998). In its in vitro interaction with synemin, desmin resembles vimentin more than GFAP because, in biochemical assays, synemin copolymerizes with desmin but binds only minimally to preformed desmin IFs (Bellin et al, 1999).…”

Section: Vimmentioning

confidence: 99%

See 1 more Smart Citation

Synemin is expressed in reactive astrocytes in neurotrauma and interacts differentially with vimentin and GFAP intermediate filament networks

Jing

Wilhelmsson

Goodwill

et al. 2007

Journal of Cell Science

View full text Add to dashboard Cite

GFAP IFs like an IF-associated protein rather than like a polymerization partner, whereas the opposite was true for synemin interaction with vimentin. In transfection experiments, synemin did not incorporate into normal, filamentous GFAP networks, but integrated into vimentin and GFAP heteropolymeric networks. Thus, alongside GFAP, vimentin and nestin, reactive astrocytes contain synemin, whose accumulation is suppressed posttranscriptionally in the absence of a polymerization partner. In astrocytes, this partner is vimentin and not GFAP, which implies a functional difference between these two type III IF proteins.

show abstract

Section: Vimmentioning

confidence: 99%

Section: Vimmentioning

confidence: 99%

Synemin is expressed in reactive astrocytes in neurotrauma and interacts differentially with vimentin and GFAP intermediate filament networks

Jing

Wilhelmsson

Goodwill

et al. 2007

Journal of Cell Science

View full text Add to dashboard Cite

show abstract

“…Skeletal muscle fibers possess heteropolymeric intermediate filaments (IFs) comprised of desmin, synemin, and paranemin (Bilak et al, 1998;Granger and Lazarides, 1980;Price and Lazarides, 1983;Schweitzer et al, 2001). These IFs are located at the periphery of myofibrillar Z-discs, interlink adjacent myofibrils at the Z-line level, and anchor onto costameres beneath the sarcolemma (Craig and Pardo, 1983;Fujimaki et al, 1986;Lazarides, 1980;Tokuyasu et al, 1983).…”

Section: Introductionmentioning

confidence: 99%

Plectin 1 links intermediate filaments to costameric sarcolemma through β-synemin, α-dystrobrevin and actin

Hijikata

Nakamura

Isokawa

et al. 2008

Journal of Cell Science

View full text Add to dashboard Cite

show abstract

“…Unlike desmin and keratins, which are small IF proteins (40 -70 kDa), synemin is large, due to its long COOH-terminal domain, and it can be expressed in either ␣ (ϳ210 kDa)-or ␤ (ϳ180 kDa)-isoforms (3,7,8), generated by alternative splicing. In addition to desmin, synemin can associate with keratin IFs and with the costameric proteins ␣-dystrobrevin, dystrophin, utrophin, vinculin, and talin, as well as with ␣-actinin at Z disks (4,17,35,40,59,90,91).…”

mentioning

confidence: 99%

Myopathic changes in murine skeletal muscle lacking synemin

García‐Pelagio

Muriel

O’Neill

et al. 2015

American Journal of Physiology-Cell Physiology

View full text Add to dashboard Cite

(IF) proteins are associated with defects in the organization of the contractile apparatus and its links to costameres, which connect the sarcomeres to the cell membrane. Here we study the role in skeletal muscle of synemin, a type IV IF protein, by examining mice null for synemin (synm-null). Synm-null mice have a mild skeletal muscle phenotype. Tibialis anterior (TA) muscles show a significant decrease in mean fiber diameter, a decrease in twitch and tetanic force, and an increase in susceptibility to injury caused by lengthening contractions. Organization of proteins associated with the contractile apparatus and costameres is not significantly altered in the synm-null. Elastimetry of the sarcolemma and associated contractile apparatus in extensor digitorum longus myofibers reveals a reduction in tension consistent with an increase in sarcolemmal deformability. Although fatigue after repeated isometric contractions is more marked in TA muscles of synm-null mice, the ability of the mice to run uphill on a treadmill is similar to controls. Our results suggest that synemin contributes to linkage between costameres and the contractile apparatus and that the absence of synemin results in decreased fiber size and increased sarcolemmal deformability and susceptibility to injury. Thus synemin plays a moderate but distinct role in fast twitch skeletal muscle. cytoskeleton; costameres; elastimetry; biomechanical properties; desmin A LARGE NUMBER OF HUMAN DISEASES, ranging from skin disorders (51), to premature aging (34, 64), to skeletal and cardiac myopathies (19,37), are linked to mutations in genes encoding intermediate filament (IF) proteins (25). Since the discovery of desmin, the major IF protein of striated muscle (49), its role and that of other IF proteins in muscle have been of keen interest to many laboratories (reviewed in 16). Our research on muscle IF proteins has addressed their role in force transmission and in organizing the sarcoplasm and stabilizing it against injury during force generation.Force generated in muscle can be transmitted radially, from the myofibrils, across the sarcolemma to the extracellular matrix and neighboring cells (11, 67). As a result, a significant amount of force is exerted on the sarcolemma and the structures that link it to the underlying contractile apparatus and the extracellular matrix. The ability of the sarcolemma with the underlying contractile apparatus to withstand the distortions caused during isotonic contractions (2, 11, 12) depends on specialized structures, termed "costameres" (66), that mediate the radial transmission of force across the sarcolemma (11). Costameres are structures at the sarcolemma of striated muscle fibers that align circumferentially around the Z disks and the M bands of the nearest myofibrils, and longitudinally, to form a rectilinear sarcolemmal network comprised of integral membrane proteins (such as dystroglycan, the sarcoglycans, and Na-K-ATPase), proteins of the extracellular matrix (such as laminin and collagen IV), and proteins of t...

show abstract

Properties of the Novel Intermediate Filament Protein Synemin and Its Identification in Mammalian Muscle

Cited by 83 publications

References 61 publications

Synemin is expressed in reactive astrocytes in neurotrauma and interacts differentially with vimentin and GFAP intermediate filament networks

Synemin is expressed in reactive astrocytes in neurotrauma and interacts differentially with vimentin and GFAP intermediate filament networks

Plectin 1 links intermediate filaments to costameric sarcolemma through β-synemin, α-dystrobrevin and actin

Myopathic changes in murine skeletal muscle lacking synemin

Contact Info

Product

Resources

About