scholarly journals Drosophila Ataxin 2-binding protein 1 marks an intermediate step in the molecular differentiation of female germline cysts

Development ◽  
2010 ◽  
Vol 137 (19) ◽  
pp. 3167-3176 ◽  
Author(s):  
O. Y. Tastan ◽  
J. Z. Maines ◽  
Y. Li ◽  
D. M. Mckearin ◽  
M. Buszczak

Author(s):  
Chad Sundberg ◽  
Monika Lakk ◽  
Sharan Paul ◽  
K. P. Figueroa ◽  
Daniel R. Scoles ◽  
...  


2010 ◽  
Vol 285 (18) ◽  
pp. 13599-13606 ◽  
Author(s):  
Guennadi Kozlov ◽  
Nozhat Safaee ◽  
Angelika Rosenauer ◽  
Kalle Gehring




1994 ◽  
Vol 297 (2) ◽  
pp. 365-372 ◽  
Author(s):  
M J Bossard ◽  
D J Bergsma ◽  
M Brandt ◽  
G P Livi ◽  
W K Eng ◽  
...  

The binding of FK506 and rapamycin to their cytosolic receptor FKBP12 is an intermediate step in the paths leading to their potent immunosuppressive properties. One of the amino acids defining the hydrophobic binding cleft for the macrocycles is Tyr82, which is thought to form a hydrogen bond with the amide oxygens of the common pipecolyl structural element within the two macrolides. To understand better the influence of this amino acid residue in catalytic activity (cis-trans peptidyl prolyl isomerization) and ligand binding properties, a Tyr82 to Leu site-specific modification of FKBP12 was prepared, purified and characterized. Kinetic experiments have demonstrated that the Tyr82 to Leu modification has a greater effect on catalytic properties than on ligand binding affinities, a result which indicates that these inhibitors may not be binding as true transition-state analogues. In an additional test for cellular function, expression of both wild-type and mutant human FKBP12 in a strain of Saccharomyces cerevisiae rendered resistant to rapamycin by deletion of the gene encoding a cytosolic rapamycin binding protein (RPB1), the yeast homologue of FKBP12, restored wild-type drug sensitivity.



2010 ◽  
Vol 52 ◽  
pp. S425
Author(s):  
S. Joshita ◽  
T. Umemura ◽  
S. Morita ◽  
A. Kamijo ◽  
M. Komatsu ◽  
...  


2012 ◽  
Vol 287 (49) ◽  
pp. 41310-41323 ◽  
Author(s):  
Yoshihiro Nihei ◽  
Daisuke Ito ◽  
Norihiro Suzuki


Development ◽  
2017 ◽  
Vol 144 (5) ◽  
pp. 905-915 ◽  
Author(s):  
Jay Prakash Shukla ◽  
Girish Deshpande ◽  
L. S. Shashidhara


2016 ◽  
Vol 27 (20) ◽  
pp. 3052-3064 ◽  
Author(s):  
Megan M. Gnazzo ◽  
Eva-Maria E. Uhlemann ◽  
Alex R. Villarreal ◽  
Masaki Shirayama ◽  
Eddie G. Dominguez ◽  
...  

The spindle midzone harbors both microtubules and proteins necessary for furrow formation and the completion of cytokinesis. However, the mechanisms that mediate the temporal and spatial recruitment of cell division factors to the spindle midzone and midbody remain unclear. Here we describe a mechanism governed by the conserved RNA-binding protein ATX-2/Ataxin-2, which targets and maintains ZEN-4 at the spindle midzone. ATX-2 does this by regulating the amount of PAR-5 at mitotic structures, particularly the spindle, centrosomes, and midbody. Preventing ATX-2 function leads to elevated levels of PAR-5, enhanced chromatin and centrosome localization of PAR-5–GFP, and ultimately a reduction of ZEN-4–GFP at the spindle midzone. Codepletion of ATX-2 and PAR-5 rescued the localization of ZEN-4 at the spindle midzone, indicating that ATX-2 mediates the localization of ZEN-4 upstream of PAR-5. We provide the first direct evidence that ATX-2 is necessary for cytokinesis and suggest a model in which ATX-2 facilitates the targeting of ZEN-4 to the spindle midzone by mediating the posttranscriptional regulation of PAR-5.





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