Genes and Development

Home Help [Feedback] [For Subscribers] [Archive] [Search] [Contents]
 QUICK SEARCH:   [advanced]


     


GENES & DEVELOPMENT 8:1160-1173, 1994
ISSN 0890-9369
This Article
Right arrow Full Text (PDF)
Right arrow References
Right arrow Alert me when this article is cited
Right arrow Alert me if a correction is posted
Right arrow Citation Map
Services
Right arrow Email this article to a friend
Right arrow Similar articles in this journal
Right arrow Similar articles in PubMed
Right arrow Alert me to new issues of the journal
Right arrow Download to citation manager
Right arrow reprints & permissions
Citing Articles
Right arrow Citing Articles via HighWire
Right arrow Citing Articles via Google Scholar
Google Scholar
Right arrow Articles by Yun, B
Right arrow Articles by Rabinow, L
Right arrow Search for Related Content
PubMed
Right arrow PubMed Citation
Right arrow Articles by Yun, B
Right arrow Articles by Rabinow, L
Social Bookmarking
 Add to CiteULike   Add to Connotea   Add to Del.icio.us   Add to Digg   Add to Reddit   Add to Technorati  
What's this?

Research Papers

The Doa locus encodes a member of a new protein kinase family and is essential for eye and embryonic development in Drosophila melanogaster.

B Yun, R Farkas, K Lee, and L Rabinow

Waksman Institute, Rutgers University, Piscataway, New Jersey 08855-0759.

Abstract

Mutations at the Darkener of apricot (Doa) locus of Drosophila cause roughened eyes and increase transcript accumulation from the retrotransposon copia up to fourfold. Cloning of the gene and sequencing of cDNAs reveals that it encodes a putative serine/threonine protein kinase. Sequence data base searches identify it is a member of a novel highly conserved protein kinase family, with homologs in humans, mice, and Saccharomyces cerevisiae, not related to each other previously. Family members are characterized by a peptide motif reading EHLAMMERILG at kinase subdomain X, which is virtually 100% identical in all homologs. We therefore refer to this new family as the LAMMER protein kinases. As predicted from its primary sequence, Doa protein possess intrinsic protein kinase activity when expressed in bacteria, as assayed via autophosphorylation. The gene is expressed throughout development, and both stage and tissue-specific RNAs are found. Its function is essential, because maternally deposited or zygotically transcribed mRNA is required for development to larval stages, and defects in segmentation and development of the nervous system are observed in embryos derived from heteroallelic mothers. Doa function is also critical to Drosophila eye development, because the organization and development of pigment cells, bristles, and photoreceptors are affected in various mutant classes. In the most extreme cases that survive to adulthood, retinal photoreceptors degenerate prior to eclosion. These results demonstrate that the kinase encoded by Doa is required at multiple stages of development, for both differentiation and maintenance of specific cell types.



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


This article has been cited by other articles:


Home page
GENES CELLSHome page
J.-i. Yomoda, M. Muraki, N. Kataoka, T. Hosoya, M. Suzuki, M. Hagiwara, and H. Kimura
Combination of Clk family kinase and SRp75 modulates alternative splicing of Adenovirus E1A.
Genes Cells, March 1, 2008; 13(3): 233 - 244.
[Abstract] [Full Text] [PDF]


Home page
J. Biol. Chem.Home page
M. Muraki, B. Ohkawara, T. Hosoya, H. Onogi, J. Koizumi, T. Koizumi, K. Sumi, J.-i. Yomoda, M. V. Murray, H. Kimura, et al.
Manipulation of Alternative Splicing by a Newly Developed Inhibitor of Clks
J. Biol. Chem., June 4, 2004; 279(23): 24246 - 24254.
[Abstract] [Full Text] [PDF]


Home page
GeneticsHome page
M. C. Babcock, R. S. Stowers, J. Leither, C. S. Goodman, and L. J. Pallanck
A Genetic Screen for Synaptic Transmission Mutants Mapping to the Right Arm of Chromosome 3 in Drosophila
Genetics, September 1, 2003; 165(1): 171 - 183.
[Abstract] [Full Text] [PDF]


Home page
GeneticsHome page
J. Z. Morris, C. Navarro, and R. Lehmann
Identification and Analysis of Mutations in bob, Doa and Eight New Genes Required for Oocyte Specification and Development in Drosophila melanogaster
Genetics, August 1, 2003; 164(4): 1435 - 1446.
[Abstract] [Full Text] [PDF]


Home page
Plant CellHome page
S. Savaldi-Goldstein, D. Aviv, O. Davydov, and R. Fluhr
Alternative Splicing Modulation by a LAMMER Kinase Impinges on Developmental and Transcriptome Expression
PLANT CELL, April 1, 2003; 15(4): 926 - 938.
[Abstract] [Full Text] [PDF]


Home page
J. Biol. Chem.Home page
R. Katsu, H. Onogi, K. Wada, Y. Kawaguchi, and M. Hagiwara
Novel SR-rich-related Protein Clasp Specifically Interacts with Inactivated Clk4 and Induces the Exon EB Inclusion of Clk
J. Biol. Chem., November 8, 2002; 277(46): 44220 - 44228.
[Abstract] [Full Text] [PDF]


Home page
J. Biol. Chem.Home page
E. Nikolakaki, R. Kohen, A. M. Hartmann, S. Stamm, E. Georgatsou, and T. Giannakouros
Cloning and Characterization of an Alternatively Spliced Form of SR Protein Kinase 1 That Interacts Specifically with Scaffold Attachment Factor-B
J. Biol. Chem., October 19, 2001; 276(43): 40175 - 40182.
[Abstract] [Full Text] [PDF]


Home page
GeneticsHome page
B. Yun, K. Lee, R. Farka, C. Hitte, and L. Rabinow
The LAMMER Protein Kinase Encoded by the Doa Locus of Drosophila Is Required in Both Somatic and Germline Cells and Is Expressed as Both Nuclear and Cytoplasmic Isoforms Throughout Development
Genetics, October 1, 2000; 156(2): 749 - 761.
[Abstract] [Full Text]


Home page
Mol. Cell. Biol.Home page
Z. Tang, T. Kuo, J. Shen, and R.-J. Lin
Biochemical and Genetic Conservation of Fission Yeast Dsk1 and Human SR Protein-Specific Kinase 1
Mol. Cell. Biol., February 1, 2000; 20(3): 816 - 824.
[Abstract] [Full Text]


Home page
J. Cell Sci.Home page
H. Menegay, M. Myers, F. Moeslein, and G. Landreth
Biochemical characterization and localization of the dual specificity kinase CLK1
J. Cell Sci., January 9, 2000; 113(18): 3241 - 3253.
[Abstract] [PDF]


Home page
J. Biol. Chem.Home page
F. M. Moeslein, M. P. Myers, and G. E. Landreth
The CLK Family Kinases, CLK1 and CLK2, Phosphorylate and Activate the Tyrosine Phosphatase, PTP-1B
J. Biol. Chem., September 17, 1999; 274(38): 26697 - 26704.
[Abstract] [Full Text] [PDF]


Home page
J. Biol. Chem.Home page
O. Nayler, F. Schnorrer, S. Stamm, and A. Ullrich
The Cellular Localization of the Murine Serine/Arginine-rich Protein Kinase CLK2 Is Regulated by Serine 141 Autophosphorylation
J. Biol. Chem., December 18, 1998; 273(51): 34341 - 34348.
[Abstract] [Full Text] [PDF]


Home page
J. Biol. Chem.Home page
K. Lee, C. Du, M. Horn, and L. Rabinow
Activity and Autophosphorylation of LAMMER Protein Kinases
J. Biol. Chem., November 1, 1996; 271(44): 27299 - 27303.
[Abstract] [Full Text] [PDF]


Home page
J. Biol. Chem.Home page
T. Kojima, T. Zama, K. Wada, H. Onogi, and M. Hagiwara
Cloning of Human PRP4 Reveals Interaction with Clk1
J. Biol. Chem., August 17, 2001; 276(34): 32247 - 32256.
[Abstract] [Full Text] [PDF]




Home Help [Feedback] [For Subscribers] [Archive] [Search] [Contents]
Genome Res. Learn. Mem.
Protein Science RNA Genes Dev.