A region of a PtK2 cell transfected with GFP-keratin 14

2009 ◽  
Vol 2009 (12) ◽  
pp. pdb.mov56-pdb.mov56
Keyword(s):  
1999 ◽  
Vol 141 (4) ◽  
pp. 747-748 ◽  
Author(s):  
Sasaki ◽  
Shimizu ◽  
Akiyama ◽  
Hiraoka ◽  
Takizawa ◽  
...  

2008 ◽  
Vol 84 (2) ◽  
pp. 406-419 ◽  
Author(s):  
Yingchun Yu ◽  
Yingjun Su ◽  
Susan R. Opalenik ◽  
Tammy Sobolik-Delmaire ◽  
Nicole F. Neel ◽  
...  

1978 ◽  
Vol 77 (3) ◽  
pp. R27 ◽  
Author(s):  
M Osborn ◽  
RE Webster ◽  
K Weber

PtK2 cells were grown on gold grids and treated with Triton X-100 in a microtubule stabilizing buffer. The resulting cytoskeletons were fixed with glutaraldehyde and subjected to the indirect immunofluorescence procedure using monospecific tubulin antibodies. Grids were examined first by fluorescence microscopy, and the display of fluorescent cytoplasmic microtubules was recorded. The grids were then stained with uranyl acetate and the display of fibrous structures recorded by electron microscopy. Thus the display of cytoplasmic microtubular structures in the light microscope and the electron microscope can be compared within the same cytoskeleton. The results show a direct correspondence of the fluorescent fibers in the light microscope with uninterrupted fibers of diameter approximately 550 A in the electron microscope. This is the diameter reported for a single microtubule decorated around its circumference by two layers of antibody molecules. Thus under optimal conditions immunofluorescence microscopy can visualize individual microtubules.


2004 ◽  
Vol 166 (4) ◽  
pp. 479-485 ◽  
Author(s):  
Nam-On Ku ◽  
Haian Fu ◽  
M. Bishr Omary

Keratins 8 and 18 (K8/18) heteropolymers may regulate cell signaling via the known K18 association with 14-3-3 proteins and 14-3-3 association with Raf-1 kinase. We characterized Raf–keratin–14-3-3 associations and show that Raf associates directly with K8, independent of Raf kinase activity or Ras–Raf interaction, and that K18 is a Raf physiologic substrate. Raf activation during oxidative and toxin exposure in cultured cells and animals disrupt keratin–Raf association in a phosphorylation-dependent manner. Mutational analysis showed that 14-3-3 residues that are essential for Raf binding also regulate 14-3-3–keratin association. Similarly, Raf phosphorylation sites that are important for binding to 14-3-3 are also essential for Raf binding to K8/18. Therefore, keratins may modulate some aspects of Raf signaling under basal conditions via sequestration by K8, akin to Raf–14-3-3 binding. Keratin-bound Raf kinase is released upon Raf hyperphosphorylation and activation during oxidative and other stresses.


2016 ◽  
Vol 48 (12) ◽  
pp. 1508-1516 ◽  
Author(s):  
Zhimiao Lin ◽  
Shuo Li ◽  
Cheng Feng ◽  
Shang Yang ◽  
Huijun Wang ◽  
...  

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