Actin-Binding Protein (ABP-280) Filamin Gene (FLN) Maps Telomeric to the Color Vision Locus (R/GCP) and Centromeric to G6PD in Xq28

Gorlin, Jed B.; Henske, Elizabeth P.; Warren, Stephen T.; Kunst, Catherine B.; D’Urso, Michele; Palmieri, Giuseppe; Hartwig, John H.; Bruns, G. A. P.; Kwiatkowski, David J.

doi:10.1006/geno.1993.1354

Cited by 36 publications

(24 citation statements)

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“…Filamin is an actin-binding protein that is found as different isoforms. Filamin-1 is a non-muscle filamin found in a wide variety of cell types (26), whereas ␥-filamin/ABP-L (27) is expressed primarily in heart and skeletal muscle (28,29). ␥-Filamin/ABP-L is also called filamin-2 and has been shown to bind ␥-and ␦-sarcoglycans, which are members of the dystrophin-glycoprotein complex (30).…”

Section: Discussionmentioning

confidence: 99%

FATZ, a Filamin-, Actinin-, and Telethonin-binding Protein of the Z-disc of Skeletal Muscle

Faulkner¹,

Pallavicini²,

Comelli³

et al. 2000

Journal of Biological Chemistry

150

115

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We report the identification and characterization of a novel 32-kDa protein expressed in skeletal muscle and located in the Z-disc of the sarcomere. We found that this protein binds to three other Z-disc proteins; therefore, we have named it FATZ, ␥-filamin/ABP-L, ␣-actinin and telethonin binding protein of the Z-disc. From yeast twohybrid experiments we are able to show that the SR3-SR4 domains of ␣-actinin 2 are required to bind the COOH-terminal region of the FATZ as does ␥-filamin/ ABP-L. Furthermore, by using a glutathione S-transferase overlay assay we find that FATZ also binds telethonin. The level of FATZ protein in muscle cells increases during differentiation, being clearly detectable before the onset of myosin. Although FATZ has no known interaction domains, it would appear to be involved in a complex network of interactions with other Z-band components. On the basis of the information known about its binding partners, we could envisage a central role for FATZ in the myofibrillogenesis. After screening our muscle expressed sequence tag data base and the public expressed sequence tag data bases, we were able to assemble two other muscle transcripts that show a high level of identity with FATZ in two different domains. Therefore, FATZ may be the first member of a small family of novel muscle proteins.The Z-disc of vertebrate striated muscle is a region where the antiparallel actin filaments spanning the sarcomere are crosslinked. This supramolecular structure plays an important role in the regulation of contraction both in skeletal and cardiac muscle. Variation of the Z-disc structure is observed during development and differentiation of muscle cells and can be correlated with specific pathological or degenerative conditions associated with muscle injuries or atrophies.The number of different protein components of the Z-disc is far from being complete, and many of the newly discovered muscle proteins appear to be localized in this region, and very generally they can be divided into two groups based on their location. In the first group are proteins that are only partially in the Z-disc while extending into other portions of the sarcomere or the sarcolemma. An example of the first group is titin that acts as a ruler for the ordered distribution of sarcomeric proteins and is particularly important in Z-disc assembly. The NH 2 -terminal portion of titin extends into the Z-disc, where two different sub-domains have been shown to interact specifically with ␣-actinin (1-3) and also with the muscle-specific protein telethonin (4). Although telethonin binds to the NH 2 -terminal domain of titin, it also acts as one of the substrates of the titin serine kinase domain that is located outside of the Z-disc (5). The second group is composed of proteins, many of which have been recently discovered and characterized, that appear to be entirely located in the Z-disc (e.g. ␣-actinin, Nspl1, telethonin, ZASP1, and CapZ). Among these proteins, ␣-actinin plays a central role by directly cross-linking the actin molecules. ...

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Section: Discussionmentioning

confidence: 99%

FATZ, a Filamin-, Actinin-, and Telethonin-binding Protein of the Z-disc of Skeletal Muscle

Faulkner¹,

Pallavicini²,

Comelli³

et al. 2000

Journal of Biological Chemistry

150

115

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“…The FLN1 gene maps to human chromosome Xq28 and is expressed in many cell types, whereas the FLN2 gene maps to human chromosome 7q32-35 and is expressed predominantly in skeletal and cardiac muscle (Gorlin et al, 1993;Maetrini et al, 1993).…”

Section: Human Fh1 Gene Maps To Chromosomementioning

confidence: 99%

Interaction of Presenilins with the Filamin Family of Actin-Binding Proteins

Zhang¹,

Han²,

McKeel

et al. 1998

J. Neurosci.

118

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Mutations in presenilin genes PS1 and PS2 account for ϳ50% of early-onset familial Alzheimer's disease (FAD). The PS1 and PS2 genes encode highly homologous transmembrane proteins related to the Caenorhabditis elegans sel-12 and spe-4 gene products. A hydrophilic loop region facing the cytoplasmic compartment is likely to be functionally important because at least 14 mutations in FAD patients have been identified in this region. We report here that the loop regions of PS1 and PS2 interact with nonmuscle filamin (actin-binding protein 280, ABP280) and a structurally related protein (filamin homolog 1, Fh1). Overexpression of PS1 appears to modify the distribution of ABP280 and Fh1 proteins in cultured cells. A monoclonal antibody recognizing ABP280 and Fh1 binds to blood vessels, astrocytes, neurofibrillary tangles, neuropil threads, and dystrophic neurites in the AD brain. Detection of ABP280/Fh1 proteins in these structures suggests that these presenilin-interacting proteins may be involved in the development of AD and that interactions between presenilins and ABP280/Fh1 may be functionally significant. The ABP280 gene is located on the human X chromosome, whereas the newly identified Fh1 gene maps to human chromosome 3. These results provide a new basis for understanding the function of presenilin proteins and further implicate cytoskeletal elements in AD pathogenesis.

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“…ABP-280 cDNA has been cloned from a HUVEC cDNA library (6) and mapped to the X chromosome (7,8). ABP-280 has sometimes been referred to as human non-muscle filamin.…”

mentioning

confidence: 99%

Human β-Filamin Is a New Protein That Interacts with the Cytoplasmic Tail of Glycoprotein Ibα

Takafuta¹,

Wu²,

Murphy³

et al. 1998

Journal of Biological Chemistry

106

101

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Actin-Binding Protein (ABP-280) Filamin Gene (FLN) Maps Telomeric to the Color Vision Locus (R/GCP) and Centromeric to G6PD in Xq28

Cited by 36 publications

References 0 publications

FATZ, a Filamin-, Actinin-, and Telethonin-binding Protein of the Z-disc of Skeletal Muscle

FATZ, a Filamin-, Actinin-, and Telethonin-binding Protein of the Z-disc of Skeletal Muscle

Interaction of Presenilins with the Filamin Family of Actin-Binding Proteins

Human β-Filamin Is a New Protein That Interacts with the Cytoplasmic Tail of Glycoprotein Ibα

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