The DOI matches its Crossref record; 1 of the 1 references it cites were found in a registry or an index.
The LIM/double zinc-finger motif functions as a protein dimerization domain.
Open accessAbstract
Protein-protein interactions resulting in dimerization and heterodimerization are of central importance in the control of gene expression and cell function. Proteins that share the 52-residue LIM/double zinc-finger domain are involved in a wide range of developmental and cellular controls. Some of these functions have been hypothesized to involve protein dimerization. In the present report we demonstrate, using both in vitro and cell-based studies, that a representative LIM protein, human cysteine-rich protein (hCRP), can efficiently homodimerize. The dimerization ability of hCRP is mapped to the LIM domains, can be transferred to an unrelated protein by fusion of a single minimal LIM/double zinc-finger segment, occurs in the absence as well as the presence of DNA, and appears to depend on coordination of two zinc atoms in the finger doublet. These observations support a specific role for protein dimerization in the function of proteins containing the LIM/double zinc-finger domain and expand the general spectrum of potential interactions mediated by zinc-finger motifs.
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Citations
Cites
The Leucine Zipper: A Hypothetical Structure Common to a New Class of DNA Binding Proteins
Landschulz, W. H., Johnson, P. F., & McKnight, S. L. (1988) · Science · doi:10.1126/science.3289117 · Cited by 3,443
Cited by
Martindale, M. Q., Pang, K., & Finnerty, J. R. (2004) · Development · doi:10.1242/dev.01119 · Cited by 396
Focal adhesion kinase in integrin-mediated signaling
Cary, L. (1999) · Frontiers in Bioscience · doi:10.2741/cary · Cited by 346
Zinc-finger transcription factors in plants
Takatsuji, H. (1998) · Cellular and Molecular Life Sciences (CMLS) · doi:10.1007/s000180050186 · Cited by 324
Muscle LIM Protein Promotes Myogenesis by Enhancing the Activity of MyoD
Kong, Y., Flick, M. J., Kudla, A. J., & Konieczny, S. F. (1997) · Molecular and Cellular Biology · doi:10.1128/mcb.17.8.4750 · Cited by 285
Komada, M., & Kitamura, N. (1995) · Molecular and Cellular Biology · doi:10.1128/mcb.15.11.6213 · Cited by 149
Metadata
- Authors
- Feuerstein, R., Wang, X., Song, D., Cooke, N. E., & Liebhaber, S. A.
- Venue
- Proceedings of the National Academy of Sciences
- Published
- 1994-10-25
- Volume
- 91
- Issue
- 22
- Pages
- 10655-10659
- ISSN
- 0027-8424 (ISSN-L)
- 1091-6490
- OpenAlex
- W2032881439
- Cited by
- 192
- References
- 1
- FWCI
- 5.76
- Type
- journal article
- Language
- en
- Open access
- green
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- Feuerstein, R., Wang, X., Song, D., Cooke, N. E., & Liebhaber, S. A. (1994). The LIM/double zinc-finger motif functions as a protein dimerization domain. Proceedings of the National Academy of Sciences. https://doi.org/10.1073/pnas.91.22.10655
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Contains information from the Semantic Scholar Academic Graph Datasets, made available under the ODC Attribution License (ODC-BY 1.0).
Semantic Scholar’s data is described in: Kinney, R., et al. (2023). The Semantic Scholar Open Data Platform. arXiv:2301.10140.
