Smooth muscle α-actinin binds tightly to fesselin and attenuates its activity toward actin polymerization

Pham, Minh; Chalovich, Joseph M.

doi:10.1007/s10974-005-9053-2

Cited by 11 publications

(10 citation statements)

References 24 publications

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“…In the case of turkey fesselin neither fesselin nor α-actinin were seen in the supernatant at 0.5 μM α-actinin (Western blot, not shown). This is consistent with high affinity (about 4 × 10 7 M −1 ) previously reported for this complex [22]. It was possible to detect α-actinin in the supernatants at 1 and 1.5 μM α-actinin concentrations indicating that the fesselin sites were saturated by 0.5 μM α-actinin.…”

Section: Resultssupporting

confidence: 91%

“…We show here that rabbit smooth muscle synaptopodin 2 binds directly to α-actinin with an affinity similar to that of fesselin [22]. As we described earlier for fesselin, the binding of synaptopodin 2 to α-actinin results in the formation of a large complex that can be isolated by centrifugation.…”

Section: Discussionsupporting

confidence: 52%

“…Fesselin binds to α-actinin and forms complexes that can be isolated by sedimentation [22]. Figure 3A shows a comparison of synaptopodin 2 with fesselin in sedimentation assays to access their relative abilities to bind to α-actinin.…”

Section: Resultsmentioning

confidence: 99%

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In vitro characterization of native mammalian smooth-muscle protein synaptopodin 2

et al. 2008

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An analysis of the primary structure of the actin binding protein fesselin revealed it to be the avian homologue of mammalian synaptopodin 2 1 [Schroeter, Beall, Heid, and Chalovich (2008) Biochem. Biophys. Res. Commun. 371, 582-586]. We isolated synaptopodin 2 from rabbit stomach and showed that it shared several key functions with fesselin. Both fesselin and synaptopodin 2 bound to Ca2+-calmodulin, α–actinin, and smooth muscle myosin. In addition, both proteins stimulated the polymerization of actin in a Ca2+-calmodulin dependent manner. Synaptopodin 2 has never before been shown to polymerize actin in the absence of α-actinin, to polymerize actin in a Ca2+-calmodulin dependent manner, or to bind to Ca2+-calmodulin, or myosin. These properties are consistent of the proposed function of synaptopodin 2 in organizing the cytoskeleton.

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Section: Resultssupporting

confidence: 91%

Section: Discussionsupporting

confidence: 52%

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In vitro characterization of native mammalian smooth-muscle protein synaptopodin 2

et al. 2008

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“…That interaction has been shown to involve the central spectrin domain repeat region of α-actinin (Pham and Chalovich 2006). In solution the affinity for α-actinin is about 4×10 7 M −1 with a stoichiometry of 1:1 (116 mM ionic strength, pH 7, 25°C).…”

Section: Ligand Bindingmentioning

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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“…Furthermore fesselin binds to several actin binding proteins including myosin (Schroeter and Chalovich 2005) and α-actinin (Pham and Chalovich 2006). Western blots using crude polyclonal antibody revealed fesselin expression in mammalian smooth, skeletal and cardiac muscle tissues.…”

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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Smooth muscle α-actinin binds tightly to fesselin and attenuates its activity toward actin polymerization

Cited by 11 publications

References 24 publications

In vitro characterization of native mammalian smooth-muscle protein synaptopodin 2

In vitro characterization of native mammalian smooth-muscle protein synaptopodin 2

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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