J. Cell Biol.
© The Rockefeller University Press
0021-9525/97/08/575/14 $2.00
Volume 138, Number 3, August 11, 1997 575-588

Molecular Characterization of abLIM, a Novel Actin-binding and Double Zinc Finger Protein

Dorothy J. Roof,^* Annmarie Hayes,^* Michael Adamian,^* Athar H. Chishti, and Tiansen Li^*

^* Berman-Gund Laboratory for the Study of Retinal Degenerations, Department of Ophthalmology, Harvard Medical School, Boston, Massachusetts 02114; and  Laboratory of Tumor Cell Biology, Department of Biomedical Research, St. Elizabeth's Medical Center, Tufts University School of Medicine, Boston, Massachusetts 02135

Molecules that couple the actin-based cytoskeleton to intracellular signaling pathways are central to the processes of cellular morphogenesis and differentiation. We have characterized a novel protein, the actin-binding LIM (abLIM) protein, which could mediate such interactions between actin filaments and cytoplasmic targets. abLIM protein consists of a COOH-terminal cytoskeletal domain that is fused to an NH₂-terminal domain consisting of four double zinc finger motifs. The cytoskeletal domain is ~50% identical to erythrocyte dematin, an actin-bundling protein of the red cell membrane skeleton, while the zinc finger domains conform to the LIM motif consensus sequence. In vitro expression studies demonstrate that abLIM protein can bind to F-actin through the dematin-like domain. Transcripts corresponding to three distinct isoforms have a widespread tissue distribution. However, a polypeptide corresponding to the full-length isoform is found exclusively in the retina and is enriched in biochemical extracts of retinal rod inner segments. abLIM protein also undergoes extensive phosphorylation in light-adapted retinas in vivo, and its developmental expression in the retina coincides with the elaboration of photoreceptor inner and outer segments. Based on the composite primary structure of abLIM protein, actin-binding capacity, potential regulation via phosphorylation, and isoform expression pattern, we speculate that abLIM may play a general role in bridging the actin-based cytoskeleton with an array of potential LIM protein-binding partners. The developmental time course of abLIM expression in the retina suggests that the retina-specific isoform may have a specialized role in the development or elaboration of photoreceptor inner and outer segments.

CiteULike    Complore    Connotea    Del.icio.us    Digg    Reddit    Technorati    What's this?

This article has been cited by other articles:

• Reiner, D. J., Jan, T. A., Boughter, J. D. Jr, Li, C.-X., Lu, L., Williams, R. W., Waters, R. S. (2008). Genetic Analysis of Tongue Size and Taste Papillae Number and Size in Recombinant Inbred Strains of Mice. Chem Senses 0: bjn025v1-bjn025 [Abstract] [Full Text]  
• Lee, A., Jimenez, A., Cui, G., Haeseleer, F. (2007). Phosphorylation of the Ca2+-Binding Protein CaBP4 by Protein Kinase C {zeta} in Photoreceptors. J. Neurosci. 27: 12743-12754 [Abstract] [Full Text]  
• George, S. P., Wang, Y., Mathew, S., Srinivasan, K., Khurana, S. (2007). Dimerization and Actin-bundling Properties of Villin and Its Role in the Assembly of Epithelial Cell Brush Borders. J. Biol. Chem. 282: 26528-26541 [Abstract] [Full Text]  
• Ohgaki, H., Kleihues, P. (2007). Genetic Pathways to Primary and Secondary Glioblastoma. Am. J. Pathol. 170: 1445-1453 [Abstract] [Full Text]  
• Barrientos, T., Frank, D., Kuwahara, K., Bezprozvannaya, S., Pipes, G. C. T., Bassel-Duby, R., Richardson, J. A., Katus, H. A., Olson, E. N., Frey, N. (2007). Two Novel Members of the ABLIM Protein Family, ABLIM-2 and -3, Associate with STARS and Directly Bind F-actin. J. Biol. Chem. 282: 8393-8403 [Abstract] [Full Text]  
• Yang, Y., Lundquist, E. A. (2005). The Actin-Binding Protein UNC-115/abLIM Controls Formation of Lamellipodia and Filopodia and Neuronal Morphogenesis in Caenorhabditis elegans. Mol. Cell. Biol. 25: 5158-5170 [Abstract] [Full Text]  
• Leonoudakis, D., Conti, L. R., Anderson, S., Radeke, C. M., McGuire, L. M. M., Adams, M. E., Froehner, S. C., Yates, J. R. III, Vandenberg, C. A. (2004). Protein Trafficking and Anchoring Complexes Revealed by Proteomic Analysis of Inward Rectifier Potassium Channel (Kir2.x)-associated Proteins. J. Biol. Chem. 279: 22331-22346 [Abstract] [Full Text]  
• Vermeulen, W., Vanhaesebrouck, P., Van Troys, M., Verschueren, M., Fant, F., Goethals, M., Ampe, C., Martins, J. C., Borremans, F. A.M. (2004). Solution structures of the C-terminal headpiece subdomains of human villin and advillin, evaluation of headpiece F-actin-binding requirements. Protein Sci. 13: 1276-1287 [Abstract] [Full Text]  
• van den Boom, J., Wolter, M., Kuick, R., Misek, D. E., Youkilis, A. S., Wechsler, D. S., Sommer, C., Reifenberger, G., Hanash, S. M. (2003). Characterization of Gene Expression Profiles Associated with Glioma Progression Using Oligonucleotide-Based Microarray Analysis and Real-Time Reverse Transcription-Polymerase Chain Reaction. Am. J. Pathol. 163: 1033-1043 [Abstract] [Full Text]  
• Grzeskowiak, R., Witt, H., Drungowski, M., Thermann, R., Hennig, S., Perrot, A., Osterziel, K. J., Klingbiel, D., Scheid, S., Spang, R., Lehrach, H., Ruiz, P. (2003). Expression profiling of human idiopathic dilated cardiomyopathy. Cardiovasc Res 59: 400-411 [Abstract] [Full Text]  
• Struckhoff, E. C., Lundquist, E. A. (2003). The actin-binding protein UNC-115 is an effector of Rac signaling during axon pathfinding in C. elegans. Development 130: 693-704 [Abstract] [Full Text]  
• Athman, R., Louvard, D., Robine, S. (2002). The Epithelial Cell Cytoskeleton and Intracellular Trafficking: III. How is villin involved in the actin cytoskeleton dynamics in intestinal cells?. Am. J. Physiol. Gastrointest. Liver Physiol. 283: G496-G502 [Abstract] [Full Text]  
• Hwang, K.-Y., Schwartz, B. S., Lee, B.-K., Strickland, P. T., Todd, A. C., Bressler, J. P. (2001). Associations of Lead Exposure and Dose Measures with Erythrocyte Protein Kinase C Activity in 212 Current Korean Lead Workers. Toxicol Sci 62: 280-288 [Abstract] [Full Text]  
• Bauer, K., Kratzer, M., Otte, M., de Quintana, K. L., Hagmann, J., Arnold, G. J., Eckerskorn, C., Lottspeich, F., Siess, W. (2000). Human CLP36, a PDZ-domain and LIM-domain protein, binds to alpha -actinin-1 and associates with actin filaments and stress fibers in activated platelets and endothelial cells. Blood 96: 4236-4245 [Abstract] [Full Text]  
• Champliaud, M.-F., Burgeson, R. E., Jin, W., Baden, H. P., Olson, P. F. (1998). cDNA Cloning and Characterization of Sciellin, a LIM Domain Protein of the Keratinocyte Cornified Envelope. J. Biol. Chem. 273: 31547-31554 [Abstract] [Full Text]  
• Marks, P., Arai, M, Bandura, J., Kwiatkowski, D. (1998). Advillin (p92): a new member of the gelsolin/villin family of actin regulatory proteins. J. Cell Sci. 111: 2129-2136 [Abstract]  
• Hagmann, J, Grob, M, Welman, A, van Willigen, G, Burger, M. (1998). Recruitment of the LIM protein hic-5 to focal contacts of human platelets. J. Cell Sci. 111: 2181-2188 [Abstract]  
• Wixler, V., Geerts, D., Laplantine, E., Westhoff, D., Smyth, N., Aumailley, M., Sonnenberg, A., Paulsson, M. (2000). The LIM-only Protein DRAL/FHL2 Binds to the Cytoplasmic Domain of Several alpha and beta Integrin Chains and Is Recruited to Adhesion Complexes. J. Biol. Chem. 275: 33669-33678 [Abstract] [Full Text]  

Home | Help | Feedback | Subscriptions | Archive | Search | Table of Contents