Caenorhabditis elegans UNC-98, a C2H2Zn finger protein, is a novel partner of UNC-97/PINCH in muscle adhesion complexes
Caenorhabditis elegans UNC-98, a C2H2Zn finger protein, is a novel partner of UNC-97/PINCH in muscle adhesion complexes
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DOI:
10.1091/mbc.e02-10-0676
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发表时间:
2003-06-01
影响因子:
3.3
通讯作者:
Benian, GM
中科院分区:
文献类型:
--
作者:
Mercer, KB;Flaherty, DB;Benian, GM
To further understand the assembly and maintenance of the muscle, contractile apparatus, we have identified a new protein, UNC-98, in the muscle of Caenorhabditis elegans. unc-98 mutants display reduced motility and a characteristic defect in muscle structure. We show that the major defect in the mutant muscle is in the M-lines and dense, bodies (Z-Iine analogs). Both functionally and compositionally, nematode M-lines and dense bodies are analogous to focal adhesions of nonmuscle cells. UNC-98 is a novel 310-residue polypeptide consisting of four C2H2 Zn fingers and several possible nuclear localization signal and nuclear export signal sequences. By use of UNC-98 antibodies and green fluorescent protein fusions (to full-length UNC-98 and UNC-98 fragments), we have shown that UNC-98 resides at M-lines, muscle cell nuclei, and possibly at dense bodies. Furthermore, we demonstrated that 1) the N-terminal 106 amino adds are both necessary and sufficient for nuclear localization, and 2) the C-terminal (fourth) Zn finger is required for localization to Wines and dense bodies. UNC-98 interacts with UNC-97, a C. elegans homolog of PINCH. We propose, that UNC-98 is both a structural component of muscle focal adhesions and a nuclear protein that influences gene expression.