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Bd, Leinweber; Rs, Fredricksen; Dr, Hoffman; Chalovich, Joseph M.

doi:10.1023/a:1005597306671

Cited by 26 publications

(42 citation statements)

References 18 publications

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“…None of these clones selfactivated in the absence of the actinin-containing pGBT9 clones, nor did they interact with a control plasmid, pVA3, containing part of murine p53 in pGBT9. Preliminary DNA sequence analysis revealed that 3c41 encoded a portion of synaptopodin, an actin-binding protein at synapses and glomerular podocytes (26), whereas 3c2 represented myopodin͞ genethonin 2, a related actin-binding protein of skeletal muscle (27). Transcript 3c8 represented a gene with no existing database entries except for ESTs.…”

Section: Identification and Cloning Of A Gene For A Skeletal Muscle ␣mentioning

confidence: 99%

Myozenin: An alpha -actinin- and gamma -filamin-binding protein of skeletal muscle Z lines

Takada¹

2001

Proceedings of the National Academy of Sciences

121

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To better understand the structure and function of Z lines, we used sarcomeric isoforms of ␣-actinin and ␥-filamin to screen a human skeletal muscle cDNA library for interacting proteins by using the yeast two-hybrid system. Here we describe myozenin (MYOZ), an ␣-actinin-and ␥-filamin-binding Z line protein expressed predominantly in skeletal muscle. Myozenin is predicted to be a 32-kDa, globular protein with a central glycine-rich domain flanked by ␣-helical regions with no strong homologies to any known genes. The MYOZ gene has six exons and maps to human chromosome 10q22.1-q22.2. Northern blot analysis demonstrated that this transcript is expressed primarily in skeletal muscle with significantly lower levels of expression in several other tissues. Antimyozenin antisera stain skeletal muscle in a sarcomeric pattern indistinguishable from that seen by using antibodies for ␣-actinin, and immunogold electron microscopy confirms localization specifically to Z lines. Thus, myozenin is a skeletal muscle Z line protein that may be a good candidate gene for limb-girdle muscular dystrophy or other neuromuscular disorders.

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Section: Identification and Cloning Of A Gene For A Skeletal Muscle ␣mentioning

confidence: 99%

Myozenin: An alpha -actinin- and gamma -filamin-binding protein of skeletal muscle Z lines

Takada¹

2001

Proceedings of the National Academy of Sciences

121

123

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“…Fesselin was purified from turkey gizzards using the method of Leinweber et al (1). The fesselin concentration was determined by the Lowry assay using bovine serum albumin as a standard.…”

Section: Protein Preparationsmentioning

confidence: 99%

Fesselin, a Synaptopodin-like Protein, Stimulates Actin Nucleation and Polymerization

Beall

Chalovich

2001

Biochemistry

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Fesselin is a proline-rich actin binding protein that has recently been isolated from smooth muscle [Leinweber, B. D., Fredricksen, R. S., Hoffman, D. R., and Chalovich, J. M. (1999) J. Muscle Res. Cell Motil. 20,[539][540][541][542][543][544][545]. Fesselin is similar to synaptopodin [Mundel, P., Heid, H. W., Mundel, T. M., Krüger, M., Reiser, J., and Kriz, W. (1997) J. Cell Biol. 139, 193-204] in terms of its size, isoelectric point, and sequence although synaptopodin is not present in smooth muscle. The function of fesselin is unknown. Evidence is presented here that fesselin accelerates the polymerization of actin. Fesselin was effective on actin isolated from either smooth or skeletal muscle at low ionic strength and in the presence of 100 mM KCl. At low ionic strength, fesselin decreased the time for 50% polymerization to about 1% of that in the absence of fesselin. The lag phase characteristic of the slow nucleation process of polymerization was eliminated as the fesselin concentration was increased from very low levels. Fesselin did not alter the critical concentration for actin but did increase the rate of elongation by ≈3-fold. The increase in elongation rate constant is insufficient to account for the total increase in polymerization rate. It is likely that fesselin stabilizes the formation of actin nuclei. Time courses of actin polymerization at varied fesselin concentrations and varied actin concentrations were simulated by increasing the rate of nucleation and both the forward and reverse rate constants for elongation.Fesselin is an actin binding protein that has recently been isolated from turkey gizzard muscle (1). Fesselin is noteworthy because of its potent ability to bundle actin and because of its similarity to synaptopodin, a protein found in telencephalic dendrites and renal podocytes but not in smooth muscle (2). Fesselin has in common with synaptopodin a similar pI (9.3), a similar mobility on SDS gels (103 and 79 kDa for fesselin and 110 kDa for synaptopodin), a high proline content, and regions of sequence homology. Antibodies directed against synaptopodin decorate actin filaments in cells forming a punctate pattern (2); this pattern is lost following depolymerization of actin with cytochalasin B. Preliminary studies with fesselin also indicate that fesselin co-localizes with α-actinin on actin filaments (3). The functions of fesselin and synaptopodin are unknown.The effect of fesselin on actin polymerization was examined because of its ability to bind to and bundle actin filaments and its high isoelectric point. The isoelectric point was a consideration because cationic substances tend to polymerize actin (4,5). Actin binding and polymerizing proteins are often basic (6), and charge neutralization may be a factor in the function of these proteins (5).The present study provides evidence that fesselin increases the rate of actin polymerization. This was seen by increases in the apparent rates of increase of both pyrene fluorescence and † Funded by NIH Grant AR35216 and a Facult...

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“…The synaptopodin family (2) consists of proline-rich basic proteins that bind to actin (3), (4, 5). Three members of the synaptopodin family have been identified and each has multiple splice forms (2).…”

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confidence: 99%

“…Three members of the synaptopodin family have been identified and each has multiple splice forms (2). Fesselin, or avian synaptopodin 2 (6,7) is the most readily purified form of synaptopodin family members (5, 8) and is the subject of the work described here. Fesselin consists of a mixture of two polypeptides with a molecular weight of 79 and 102 kDa.…”

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confidence: 99%

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Organization of F-Actin by Fesselin (avian smooth muscle synaptopodin 2)

et al. 2013

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Fesselin or avian synaptopodin 2 is a member of the synaptopodin family of actin binding proteins. Fesselin promotes G-actin polymerization and the formation of large actin complexes that can be collected by centrifugation at low speed. Because of the potential role of fesselin in some cancers and its effects on actin we further investigated the effect of fesselin on actin. Fesselin initiated actin polymerization at a variety of conditions including the virtual absence of salt. Actin filaments formed at low salt in the presence of fesselin were similar to filaments polymerized in the presence of 100 mM KCl. In both cases the filaments were long and straight with a common orientation. Highly ordered actin bundles formed with increasing times of incubation. Blockers of actin growth at the barbed end (cytochalasin D and CapZ) did not prevent fesselin from polymerizing actin. Low concentrations of fesselin increased the critical concentration of actin. Both observations are consistent with preferential growth at the pointed end of actin filaments. These results indicate a role of fesselin in organizing cellular actin. These and other results indicate that fesselin is part of a cellular actin organizing center.

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Cited by 26 publications

References 18 publications

Myozenin: An alpha -actinin- and gamma -filamin-binding protein of skeletal muscle Z lines

Myozenin: An alpha -actinin- and gamma -filamin-binding protein of skeletal muscle Z lines

Fesselin, a Synaptopodin-like Protein, Stimulates Actin Nucleation and Polymerization

Organization of F-Actin by Fesselin (avian smooth muscle synaptopodin 2)

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