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| Content Provider | World Health Organization (WHO)-Global Index Medicus |
|---|---|
| Author | Musunuru, Kiran Farina, Kim L. Huttelmaier, Stefan Darnell, Robert Singer, Robert H. |
| Description | Author Affiliation: Farina KL ( Department of Anatomy and Structural Biology, Albert Einstein College of Medicine, Bronx, NY 10461, USA.) |
| Abstract | Chicken embryo fibroblasts (CEFs) localize β-actin mRNA to their lamellae, a process important for the maintenance of cell polarity and motility. The localization of β-actin mRNA requires a cis localization element (zipcode) and involves zipcode binding protein 1 (ZBP1), a protein that specifically binds to the zipcode. Both localize to the lamellipodia of polarized CEFs. ZBP1 and its homologues contain two $NH_{2}-terminal$ RNA recognition motifs (RRMs) and four COOH-terminal hnRNP K homology (KH) domains. By using ZBP1 truncations fused to GFP in conjunction with in situ hybridization analysis, we have determined that KH domains three and four were responsible for granule formation and cytoskeletal association. When the $NH_{2}$ terminus was deleted, granules formed by the KH domains alone did not accumulate at the leading edge, suggesting a role for the $NH_{2}$ terminus in targeting transport granules to their destination. RNA binding studies were used to show that the third and fourth KH domains, not the RRM domains, bind the zipcode of β-actin mRNA. Overexpression of the four KH domains or certain subsets of these domains delocalized β-actin mRNA in CEFs and inhibited fibroblast motility, demonstrating the importance of ZBP1 function in both β-actin mRNA localization and cell motility. |
| ISSN | 00219525 |
| e-ISSN | 15408140 |
| Journal | The Journal of Cell Biology |
| Issue Number | 1 |
| Volume Number | 160 |
| Language | English |
| Publisher | Rockefeller University Press (United States) |
| Publisher Date | 2003-01-06 |
| Publisher Place | United States |
| Access Restriction | Open |
| Subject Keyword | Actins Metabolism Cytoskeleton RNA, Messenger RNA-Binding Proteins Chemistry Genetics Amino Acid Sequence Animals Avian Proteins Cell Movement Chick Embryo Dose-Response Relationship, Drug Gene Deletion Glutathione Transferase In Situ Hybridization In Situ Hybridization, Fluorescence Microscopy, Fluorescence Molecular Sequence Data Phenotype Precipitin Tests Protein Structure, Tertiary RNA Recombinant Proteins Reverse Transcriptase Polymerase Chain Reaction Sequence Homology, Amino Acid Transcription, Genetic Transfection Research Support, U.S. Gov't, P.H.S. Cell Biology |
| Content Type | Text |
| Resource Type | Article |
| Subject | Cell Biology Medicine |
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