Molecular characterization of abLIM, a novel actin-binding and double zinc finger protein

110Citations
Citations of this article
75Readers
Mendeley users who have this article in their library.
Get full text

Abstract

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.

References Powered by Scopus

Cleavage of structural proteins during the assembly of the head of bacteriophage T4

219953Citations
N/AReaders
Get full text

Basic local alignment search tool

78874Citations
N/AReaders
Get full text

Electrophoretic transfer of proteins from polyacrylamide gels to nitrocellulose sheets: Procedure and some applications

47832Citations
N/AReaders
Get full text

Cited by Powered by Scopus

Genetic pathways to primary and secondary glioblastoma

1160Citations
N/AReaders
Get full text

LIM domains: Multiple roles as adapters and functional modifiers in protein interactions

536Citations
N/AReaders
Get full text

Characterization of gene expression profiles associated with glioma progression using oligonucleotide-based microarray analysis and real-time reverse transcription-polymerase chain reaction

275Citations
N/AReaders
Get full text

Register to see more suggestions

Mendeley helps you to discover research relevant for your work.

Already have an account?

Cite

CITATION STYLE

APA

Roof, D. J., Hayes, A., Adamian, M., Chishti, A. H., & Li, T. (1997). Molecular characterization of abLIM, a novel actin-binding and double zinc finger protein. Journal of Cell Biology, 138(3), 575–588. https://doi.org/10.1083/jcb.138.3.575

Readers over time

‘09‘10‘11‘12‘13‘14‘15‘16‘17‘18‘19‘20‘21‘22‘23‘24‘250481216

Readers' Seniority

Tooltip

PhD / Post grad / Masters / Doc 34

63%

Researcher 12

22%

Professor / Associate Prof. 7

13%

Lecturer / Post doc 1

2%

Readers' Discipline

Tooltip

Agricultural and Biological Sciences 20

42%

Biochemistry, Genetics and Molecular Bi... 18

38%

Nursing and Health Professions 6

13%

Medicine and Dentistry 4

8%

Article Metrics

Tooltip
Mentions
References: 2

Save time finding and organizing research with Mendeley

Sign up for free
0