title: The Drosophila Fry protein interacts with Trc and is highly mobile in vivo.
abstract: BACKGROUND
  Cell polarity is a common feature of eukaryotic cells. The NDR kinases have been found to regulate polarized growth in both animal cells and fungi. Drosophila Tricornered is an NDR kinase that is essential for the normal polarized growth of extensions of epidermal cells and for the tiling and branching of dendrites of da sensory neurons. Tricornered function requires interacting with the large Furry protein (3479 amino acid).
  
  
  RESULTS
  We constructed a furry (fry) transgene and established that it rescued the lethality of fry null mutations. The encoded protein was tagged at both its amino and carboxy termini and this allowed us to demonstrate that the protein existed as an uncleaved protein in vivo. We used the C terminal GFP tag to follow the protein in vivo and found it to be highly mobile. Interestingly Fry accumulated at the distal tip of growing bristles. We established that Fry and Trc could be co-immunoprecipitated from wing discs.
  
  
  CONCLUSIONS
  The mobility of Fry in both bristles and dendrites suggests that it could function in directing/mediating the intracellular transport needed for polarized growth. Our observations that full length Fry and Trc show only partial co-localization in growing bristles while an amino terminal fragment of Fry shows close to complete co-localization with Trc suggests that the interaction between these proteins is transient and regulated.
authors.affiliation: Biology Department, Cell Biology Department, Cancer Center, Morphogenesis and Regenerative Medicine Institute, University of Virginia, Charlottesville, VA 22903, USA.
authors.forename: Xiaolan
authors.initials: X
authors.lastname: Fang
authors.forename: Qiuheng
authors.initials: Q
authors.lastname: Lu
authors.forename: Kazou
authors.initials: K
authors.lastname: Emoto
authors.forename: Paul N
authors.initials: PN
authors.lastname: Adler
mesh_terms: D000595:Amino Acid Sequence; D000818:Animals; D016764:Cell Polarity; D004251:DNA Transposable Elements; D029721:Drosophila Proteins / Q000737:chemistry / Q000378:metabolism*; D004331:Drosophila melanogaster / Q000196:embryology / Q000378:metabolism*; D005804:Genes, Lethal; D008969:Molecular Sequence Data; D054730:Protein Interaction Domains and Motifs; D017346:Protein Serine-Threonine Kinases / Q000737:chemistry / Q000378:metabolism*; D016415:Sequence Alignment; D014921:Wings, Animal / Q000378:metabolism
chemical_list: D004251:DNA Transposable Elements; D029721:Drosophila Proteins; C436143:fry protein, Drosophila; C419769:trc protein, Drosophila; D017346:Protein Serine-Threonine Kinases
references.citation: FASEB J. 1995 May;9(8):576-96
references.pmid: 7768349
references.citation: Mol Biol Cell. 2005 Feb;16(2):689-700
references.pmid: 15591127
references.citation: J Proteome Res. 2008 Apr;7(4):1675-82
references.pmid: 18327897
references.citation: Mol Cell. 2007 Feb 23;25(4):625-34
references.pmid: 17317633
references.citation: Mol Biol Cell. 2003 Oct;14(10):3953-66
references.pmid: 14517310
references.citation: Mol Biol Cell. 2000 Sep;11(9):3177-90
references.pmid: 10982409
references.citation: Cell. 2001 Dec 14;107(6):739-50
references.pmid: 11747810
references.citation: Mol Biol Cell. 2005 Sep;16(9):4139-52
references.pmid: 15975907
references.citation: Mol Biol Cell. 2006 Sep;17(9):4080-92
references.pmid: 16822837
references.citation: Proc Natl Acad Sci U S A. 2001 Jun 19;98(13):7325-30
references.pmid: 11404483
references.citation: EMBO J. 2002 Sep 16;21(18):4863-74
references.pmid: 12234926
references.citation: Development. 2001 Jul;128(14):2793-802
references.pmid: 11526084
references.citation: Proc Natl Acad Sci U S A. 1998 Jun 23;95(13):7526-31
references.pmid: 9636183
references.citation: EMBO J. 2000 Sep 1;19(17):4524-32
references.pmid: 10970846
references.citation: Cell. 2004 Oct 15;119(2):245-56
references.pmid: 15479641
references.citation: Cell. 2005 Mar 11;120(5):675-85
references.pmid: 15766530
references.citation: Mol Biol Cell. 2003 Sep;14(9):3782-803
references.pmid: 12972564
references.citation: Genetics. 2000 Dec;156(4):1817-28
references.pmid: 11102376
references.citation: Mol Biol Cell. 2002 Feb;13(2):503-14
references.pmid: 11854408
references.citation: Curr Biol. 2009 Apr 28;19(8):675-81
references.pmid: 19327996
references.citation: Mol Cell Biol. 2005 Sep;25(18):8259-72
references.pmid: 16135814
references.citation: Nature. 2006 Sep 14;443(7108):210-3
references.pmid: 16906135
references.citation: Mol Cell Biol. 2001 Apr;21(7):2449-62
references.pmid: 11259593
references.citation: J Cell Sci. 2003 Jan 1;116(Pt 1):125-35
references.pmid: 12456722
references.citation: Mol Cell Biol. 1998 Apr;18(4):2100-7
references.pmid: 9528782
references.citation: J Cell Biol. 2002 Sep 2;158(5):885-900
references.pmid: 12196508