The actin binding protein, fesselin, is a member of the synaptopodin family

Schroeter, Mechthild M.; Beall, Brent; Heid, Hans; Chalovich, Joseph M.

doi:10.1016/j.bbrc.2008.04.134

Cited by 10 publications

(15 citation statements)

References 23 publications

(28 reference statements)

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“…35 The avian smooth muscle homologue, fesselin, 36,37 and the Synpo2 gene splice variant, myopodin, which is mainly expressed in skeletal muscle 38 have been studied in more detail. Both fesselin and myopodin have been demonstrated to bind to actin filaments and participate in actin polymerization by formation of actin bundles.…”

Section: Discussionmentioning

confidence: 99%

Regulation of Smooth Muscle Dystrophin and Synaptopodin 2 Expression by Actin Polymerization and Vascular Injury

Turczyńska

Swärd

Hien

et al. 2015

ATVB

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Objective-Actin dynamics in vascular smooth muscle is known to regulate contractile differentiation and may play a role in the pathogenesis of vascular disease. However, the list of genes regulated by actin polymerization in smooth muscle remains incomprehensive. Thus, the objective of this study was to identify actin-regulated genes in smooth muscle and to demonstrate the role of these genes in the regulation of vascular smooth muscle phenotype. Approach and Results-Mouse aortic smooth muscle cells were treated with an actin-stabilizing agent, jasplakinolide, and analyzed by microarrays. Several transcripts were upregulated including both known and previously unknown actin-regulated genes. Dystrophin and synaptopodin 2 were selected for further analysis in models of phenotypic modulation and vascular disease. These genes were highly expressed in differentiated versus synthetic smooth muscle and their expression was promoted by the transcription factors myocardin and myocardin-related transcription factor A. Furthermore, the expression of both synaptopodin 2 and dystrophin was significantly reduced in balloon-injured human arteries. Finally, using a dystrophin mutant mdx mouse and synaptopodin 2 knockdown, we demonstrate that these genes are involved in the regulation of smooth muscle differentiation and function. Conclusions-This

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Section: Discussionmentioning

confidence: 99%

Regulation of Smooth Muscle Dystrophin and Synaptopodin 2 Expression by Actin Polymerization and Vascular Injury

Turczyńska

Swärd

Hien

et al. 2015

ATVB

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“…Isolated synaptopodin 2 generally contains two polypeptide chains with apparent molecular masses on SDS gels of 79 and 102 kDa (Leinweber et al 1999). Synaptopodin 2 has also been prepared from rabbit stomach tissue with lower yields than from chicken or turkey gizzards (Schroeter et al 2008).…”

Section: Physical Properties and Isolationmentioning

confidence: 99%

Synaptopodin family of natively unfolded, actin binding proteins: physical properties and potential biological functions

Chalovich

Schroeter

2010

Biophys Rev

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The synaptopodin family of proteins consists of at least 3 members: synaptopodin, the synaptopodin 2 proteins, and the synaptopodin 2-like proteins. Each family member has at least 3 isoforms that are produced by alternative splicing. Synaptopodin family members are basic proteins that are rich in proline and have little regular 2° or 3° structure at physiological temperature, pH and ionic strength. Like other natively unfolded proteins, synaptopodin family members have multiple binding partners including actin and other actin-binding proteins. Several members of the synaptopodin family have been shown to stimulate actin polymerization and to bundle actin filaments either on their own or in collaboration with other proteins. Synaptopodin 2 has been shown to accelerate nucleation of actin filament formation and to induce actin bundling. The actin polymerization activity is inhibited by Ca-calmodulin. Synaptopodin 2 proteins are localized in Z-bands of striated and heart muscle and dense bodies of smooth muscle cells. Depending on the developmental status and stress, at least one member of the synaptopodin family can occupy nuclei of some cells. Members of the synaptopodin 2 subfamily have been implicated in cancers.

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“…MALDI-TOF MS fingerprint analysis confirmed the presence of fesselin in each band detected by the anti-fesselin antibody. The presence of multiple species of fesselin in gizzard smooth muscle is due to different splicing of the fesselin gene (Schroeter et al, 2008). …”

Section: Resultsmentioning

confidence: 99%

“…Fesselin is an avian homologue of mammalian synaptopodin 2 (Schroeter et al 2008) and shares several biophysical features with synaptopodin and synaptopodin 2 (myopodin) such as an isoelectric point of 9.3 and similar molecular weights (Leinweber et al 1999). In vitro studies indicate that fesselin stimulates actin polymerization by increasing actin nucleation (Beall and Chalovich 2001).…”

Section: Introductionmentioning

confidence: 99%

Localization of the actin-binding protein fesselin in chicken smooth muscle

Renegar

Chalovich

Leinweber

et al. 2008

Histochem Cell Biol

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This report compares cellular localization of fesselin in chicken smooth, skeletal and cardiac muscle tissues using affinity purified polyclonal fesselin antibodies. Western blot analyses revealed large amounts of fesselin in gizzard smooth muscle with lower amounts in skeletal and cardiac muscle. In gizzard, fesselin was detected by immunofluorescence as discrete cytoplasmic structures. Fesselin did not co-localize with talin, vinculin or caveolin indicating that fesselin is not associated with dense bands or caveolar regions of the cell membrane. Immunoelectron microscopy established localization of fesselin within dense bodies. Since dense bodies function as anchorage points for actin and desmin in smooth muscle cells, fesselin may be involved in establishing cytoskeletal structure in this tissue. In skeletal muscle, fesselin was associated with desmin in regularly space bands distributed along the length of muscle fibers suggesting localization to the Z-line. Infrequently, this banding pattern was observed in heart tissues as well. Localization at the Z-line of skeletal and cardiac muscle suggests a role in contraction of these tissues.

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The actin binding protein, fesselin, is a member of the synaptopodin family

Cited by 10 publications

References 23 publications

Regulation of Smooth Muscle Dystrophin and Synaptopodin 2 Expression by Actin Polymerization and Vascular Injury

Regulation of Smooth Muscle Dystrophin and Synaptopodin 2 Expression by Actin Polymerization and Vascular Injury

Synaptopodin family of natively unfolded, actin binding proteins: physical properties and potential biological functions

Localization of the actin-binding protein fesselin in chicken smooth muscle

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