Snapping of the Carboxyl Terminal Tail of the Catalytic Subunit of PKA onto Its Core:  Characterization of the Sites by Mutagenesis†

Biochemistry ◽  
2000 ◽  
Vol 39 (18) ◽  
pp. 5366-5373 ◽  
Author(s):  
Michael Batkin ◽  
Iris Schvartz ◽  
Shmuel Shaltiel
1991 ◽  
Vol 266 (21) ◽  
pp. 13770-13776
Author(s):  
J.R. Reeve ◽  
V. Eysselein ◽  
G.A. Eberlein ◽  
P. Chew ◽  
F.J. Ho ◽  
...  
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1991 ◽  
Vol 11 (10) ◽  
pp. 5113-5124 ◽  
Author(s):  
H Wu ◽  
A B Reynolds ◽  
S B Kanner ◽  
R R Vines ◽  
J T Parsons

Transformation of cells by the src oncogene results in elevated tyrosine phosphorylation of two related proteins, p80 and p85 (p80/85). Immunostaining with specific monoclonal antibodies revealed a striking change of subcellular localization of p80/85 in src-transformed cells. p80/85 colocalizes with F-actin in peripheral extensions of normal cells and rosettes (podosomes) of src-transformed cells. Sequence analysis of cDNA clones encoding p80/85 revealed an amino-terminal domain composed of six copies of a direct tandem repeat, each repeat containing 37 amino acids, a carboxyl-terminal SH3 domain, and an interdomain region composed of a highly charged acidic region and a region rich in proline, serine, and threonine. The multidomain structure of p80/85 and its colocalization with F-actin in normal and src-transformed cells suggest that these proteins may associate with components of the cytoskeleton and contribute to organization of cell structure.


1999 ◽  
Vol 274 (35) ◽  
pp. 24593-24601 ◽  
Author(s):  
Michael B. Wheeler ◽  
Richard W. Gelling ◽  
Simon A. Hinke ◽  
Ba Tu ◽  
Raymond A. Pederson ◽  
...  

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