How does Protein Phosphorylation Control Protein-Protein Interactions in the Photosynthetic Membrane?

1990 ◽  
pp. 1875-1878
Author(s):  
John F. Allen
Keyword(s):  
Protein Phosphorylation ◽  
Protein Interactions ◽  
Protein Protein Interactions ◽  
Photosynthetic Membrane ◽  
Control Protein

Site-specific recombination by φC31 integrase and other large serine recombinases

2010 ◽  
Vol 38 (2) ◽  
pp. 388-394 ◽  
Author(s):  
Margaret C.M. Smith ◽  
William R.A. Brown ◽  
Andrew R. McEwan ◽  
Paul A. Rowley
Keyword(s):  
Protein Interactions ◽  
Protein Protein Interactions ◽  
Serine Recombinases ◽  
Tyrosine Recombinases ◽  
Dna Binding Sites ◽  
Attachment Sites ◽  
Φc31 Integrase ◽  
Related Proteins ◽  
Control Protein

Most temperate phages encode an integrase for integration and excision of the prophage. Integrases belong either to the λ Int family of tyrosine recombinases or to a subgroup of the serine recombinases, the large serine recombinases. Integration by purified serine integrases occurs efficiently in vitro in the presence of their cognate (~50 bp) phage and host attachment sites, attP and attB respectively. Serine integrases require an accessory protein, Xis, to promote excision, a reaction in which the products of the integration reaction, attL and attR, recombine to regenerate attP and attB. Unlike other directional recombinases, serine integrases are not controlled by proteins occupying accessory DNA-binding sites. Instead, it is thought that different integrase conformations, induced by binding to the DNA substrates, control protein–protein interactions, which in turn determine whether recombination proceeds. The present review brings together the evidence for this model derived from the studies on φC31 integrase, Bxb1 integrase and other related proteins.

scholarly journals Development of Bispecific Molecules for the In Situ Detection of Protein-Protein Interactions and Protein Phosphorylation

2014 ◽  
Vol 21 (3) ◽  
pp. 357-368 ◽  
Author(s):  
Jan van Dieck ◽  
Volker Schmid ◽  
Dieter Heindl ◽  
Sebastian Dziadek ◽  
Michael Schraeml ◽  
...  
Keyword(s):  
Protein Phosphorylation ◽  
Protein Interactions ◽  
Protein Protein Interactions ◽  
In Situ Detection

scholarly journals Learning from each other: ABC transporter regulation by protein phosphorylation in plant and mammalian systems

2015 ◽  
Vol 43 (5) ◽  
pp. 966-974 ◽  
Author(s):  
Bibek Aryal ◽  
Christophe Laurent ◽  
Markus Geisler
Keyword(s):  
Protein Phosphorylation ◽  
Protein Interactions ◽  
Abc Transporters ◽  
Higher Plants ◽  
Multi Drug Resistance ◽  
Protein Protein Interactions ◽  
Regulatory Domains ◽  
Transporter Family ◽  
Hsp 90 ◽  
Post Transcriptional Regulation

The ABC (ATP-binding cassette) transporter family in higher plants is highly expanded compared with those of mammalians. Moreover, some members of the plant ABC subfamily B (ABCB) display very high substrate specificity compared with their mammalian counterparts that are often associated with multi-drug resistance phenomena. In this review, we highlight prominent functions of plant and mammalian ABC transporters and summarize our knowledge on their post-transcriptional regulation with a focus on protein phosphorylation. A deeper comparison of regulatory events of human cystic fibrosis transmembrane conductance regulator (CFTR) and ABCB1 from the model plant Arabidopsis reveals a surprisingly high degree of similarity. Both physically interact with orthologues of the FK506-binding proteins that chaperon both transporters to the plasma membrane in an action that seems to involve heat shock protein (Hsp)90. Further, both transporters are phosphorylated at regulatory domains that connect both nt-binding folds. Taken together, it appears that ABC transporters exhibit an evolutionary conserved but complex regulation by protein phosphorylation, which apparently is, at least in some cases, tightly connected with protein–protein interactions (PPI).

Sign in / Sign up

Export Citation Format

Share Document