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© Emeline Camand
Marquage par immunofluorescence d'astrocytes tumoraux ou astrocytomes (lignée cellulaire humaine U373), montrant en rouge, APC et en vert, la tubuline des microtubules. APC est un supresseur de tumeur qui est impliqué dans la polarisation des astrocytes normaux. La localisation d'APC est altérée dans des lignées de gliomes. Pour essayer de corriger, les dérèglements observés lors de la migration des cellules d'astrocytes tumuraux ou gliomes on cherche à connaitre les mécanismes moléculaires fondamentaux qui controlent la polarisation et la migration cellulaire.
Publication : Molecular microbiology

In vitro interaction between components of the inner membrane complex of the maltose ABC transporter of Escherichia coli: modulation by ATP

Scientific Fields
Diseases
Organisms
Applications
Technique

Published in Molecular microbiology - 01 Oct 1998

Mourez M, Jéhanno M, Schneider E, Dassa E

Link to Pubmed [PMID] – 9791180

Mol. Microbiol. 1998 Oct;30(2):353-63

Interactions between domains of ATP-binding cassette (ABC) transporters are of great functional importance and yet are poorly understood. To gain further knowledge of these protein-protein interactions, we studied the inner membrane complex of the maltose transporter of Escherichia coli. We focused on interactions between the nucleotide-binding protein, MalK, and the transmembrane proteins, MalF and MalG. We incubated purified MalK with inverted membrane vesicles containing MalF and MalG. MalK bound specifically to MalF and MalG and reconstituted a functional complex. We used this approach and limited proteolysis with trypsin to show that binding and hydrolysis of ATP, inducing conformational changes in MalK, modulate its interaction with MalF and MalG. MalK in the reconstituted complex was less sensitive to protease added from the cytoplasmic side of the membrane, and one proteolytic cleavage site located in the middle of a putative helical domain of MalK was protected. These results suggest that the putative helical domain of the nucleotide-binding domains is involved, through its conformational changes, in the coupling between the transmembrane domains and ATP binding/hydrolysis at the nucleotide-binding domains.

http://www.ncbi.nlm.nih.gov/pubmed/9791180