Structural and functional diversity of novel coronin 1C (CRN2) isoforms in muscle.
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Structural and functional diversity of novel coronin 1C (CRN2) isoforms in muscle. / Xavier, Charles-Peter; Rastetter, Raphael H; Stumpf, Maria; Rosentreter, André; Müller, Rolf; Reimann, Jens; Cornfine, Susanne; Linder, Stefan; van Vliet, Vanessa; Hofmann, Andreas; Morgan, Reginald O; Fernandez, Maria-Pilar; Schröder, Rolf; Noegel, Angelika A; Clemen, Christoph S.
In: J MOL BIOL, Vol. 393, No. 2, 2, 2009, p. 287-299.Research output: SCORING: Contribution to journal › SCORING: Journal article › Research › peer-review
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TY - JOUR
T1 - Structural and functional diversity of novel coronin 1C (CRN2) isoforms in muscle.
AU - Xavier, Charles-Peter
AU - Rastetter, Raphael H
AU - Stumpf, Maria
AU - Rosentreter, André
AU - Müller, Rolf
AU - Reimann, Jens
AU - Cornfine, Susanne
AU - Linder, Stefan
AU - van Vliet, Vanessa
AU - Hofmann, Andreas
AU - Morgan, Reginald O
AU - Fernandez, Maria-Pilar
AU - Schröder, Rolf
AU - Noegel, Angelika A
AU - Clemen, Christoph S
PY - 2009
Y1 - 2009
N2 - Coronin 1C (synonyms: coronin-3, CRN2), a WD40 repeat-containing protein involved in cellular actin dynamics, is ubiquitously expressed in human tissues. Here, we report on the identification and functional characterization of two novel coronin 1C isoforms, referred to as CRN2i2 and CRN2i3, which also associate with F-actin. Analyses of the coronin 1C gene disclosed a single promoter containing binding sites for myogenic regulatory factors and an alternative first exon 1b present in intron 1, which give rise to the novel isoforms. Chromatin immunoprecipitation studies demonstrate MyoD binding to a region of the CRN2 gene, which contains a highly conserved E-box element in exon 1a. Gel-filtration assays suggest that the largest isoform 3 exists as a monomer, in contrast to isoform 1 and isoform 2 appearing as trimers. CRN2i3, which can be induced by MyoD, is exclusively expressed in well-differentiated myoblasts as well as in mature skeletal muscle tissue. In human skeletal muscle, CRN2i3 is a novel component of postsynaptic neuromuscular junctions and thin filaments of myofibrils. Together, our findings postulate a role for CRN2 isoforms in the structural and functional organization of F-actin in highly ordered protein complexes.
AB - Coronin 1C (synonyms: coronin-3, CRN2), a WD40 repeat-containing protein involved in cellular actin dynamics, is ubiquitously expressed in human tissues. Here, we report on the identification and functional characterization of two novel coronin 1C isoforms, referred to as CRN2i2 and CRN2i3, which also associate with F-actin. Analyses of the coronin 1C gene disclosed a single promoter containing binding sites for myogenic regulatory factors and an alternative first exon 1b present in intron 1, which give rise to the novel isoforms. Chromatin immunoprecipitation studies demonstrate MyoD binding to a region of the CRN2 gene, which contains a highly conserved E-box element in exon 1a. Gel-filtration assays suggest that the largest isoform 3 exists as a monomer, in contrast to isoform 1 and isoform 2 appearing as trimers. CRN2i3, which can be induced by MyoD, is exclusively expressed in well-differentiated myoblasts as well as in mature skeletal muscle tissue. In human skeletal muscle, CRN2i3 is a novel component of postsynaptic neuromuscular junctions and thin filaments of myofibrils. Together, our findings postulate a role for CRN2 isoforms in the structural and functional organization of F-actin in highly ordered protein complexes.
M3 - SCORING: Zeitschriftenaufsatz
VL - 393
SP - 287
EP - 299
JO - J MOL BIOL
JF - J MOL BIOL
SN - 0022-2836
IS - 2
M1 - 2
ER -