ArticleMolecular and cellular biology1984
Expression of the intermediate-filament-associated protein synemin in chicken lens cells.
Article in Molecular and cellular biology, 1984. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 7 papers.
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Who cites it
7 citing papers in PubMed, 40 citations in OpenAlex.
- Synemin promotes AKT-dependent glioblastoma cell proliferation by antagonizing PP2A.Molecular biology of the cell · 2012Article
- Lens intermediate filaments.Experimental eye research · 2009Review
- Cytokeratin expression and early lens development.Anatomy and embryology · 1992Article
- Overexpression of the vimentin gene in transgenic mice inhibits normal lens cell differentiation.The Journal of cell biology · 1989Article
- Expression of the chicken vimentin gene in transgenic mice: efficient assembly of the avian protein into the cytoskeleton.Proceedings of the National Academy of Sciences of the United States of America · 1989Article
- Cytoskeletons of retinal pigment epithelial cells: interspecies differences of expression patterns indicate independence of cell function from the specific complement of cytoskeletal proteins.Cell and tissue research · 1988Article
- Cytoskeleton-associated plectin: in situ localization, in vitro reconstitution, and binding to immobilized intermediate filament proteins.The Journal of cell biology · 1988Article
Corrections and comments
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Authors and funding
2 authors at 1 institution in 1 country.
Funding
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Abstract
Synemin, a 230-kilodalton polypeptide component of avian muscle and erythrocyte intermediate filaments, is also found in association with the vimentin filaments of lens tissue. In chicken lens cells, synemin is bound to the core vimentin polymer with the same 180-nm periodicity that it exhibits in erythrocytes. Its solubility properties are characteristic of those of intermediate filaments in general and similar to those of synemin in muscle cells and erythrocytes. Synemin appears at an early stage of lens development and undergoes a dramatic accumulation as the epithelial cells elongate and differentiate into fiber cells. In contrast to synemin in cultured skeletal muscle, lens synemin is not confined to postmitotic, terminally differentiating cells but is present in proliferative cells as well. It is lost from the fibers near the center of the lens, as are many other cellular structures including intermediate filaments. These findings provide new information about the occurrence and expression of avian synemin and new insight regarding its presumptive role as a modulator of intermediate-filament function.
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