EspF of enteropathogenic Escherichia coli binds sorting nexin 9.
EspF of enteropathogenic Escherichia coli targets mitochondria and subverts a number of cellular functions. EspF consists of six putative Src homology 3 (SH3) domain binding motifs. In this study we identified sorting nexin 9 (SNX9) as a host cell EspF binding partner protein, which binds EspF via its amino-terminal SH3 region. Coimmunoprecipitation and confocal microscopy showed specific EspF-SNX9 interaction and non-mitochondrial protein colocalization in infected epithelial cells.
Marchès
Oliver
O
Flowers Building, Imperial College London, London SW7 2AZ, United Kingdom.
Batchelor
Miranda
M
Shaw
Robert K
RK
Patel
Amit
A
Cummings
Nicola
N
Nagai
Takeshi
T
Sasakawa
Chihiro
C
Carlsson
Sven R
SR
Lundmark
Richard
R
Cougoule
Celine
C
Caron
Emmanuelle
E
Knutton
Stuart
S
Connerton
Ian
I
Frankel
Gad
G
D020816:Amino Acid Motifs; D002352:Carrier Proteins / Q000737:chemistry / Q000378:metabolism*; D004847:Epithelial Cells / Q000737:chemistry / Q000382:microbiology; D029968:Escherichia coli Proteins / Q000737:chemistry / Q000378:metabolism*; D006367:HeLa Cells; D006801:Humans; D047468:Immunoprecipitation; D047908:Intracellular Signaling Peptides and Proteins; D018613:Microscopy, Confocal; D011485:Protein Binding; D058305:Sorting Nexins; D033921:Vesicular Transport Proteins; D018909:src Homology Domains
D002352:Carrier Proteins; D029968:Escherichia coli Proteins; C489109:EspFU protein, E coli; D047908:Intracellular Signaling Peptides and Proteins; C400533:SNX9 protein, human; D058305:Sorting Nexins; D033921:Vesicular Transport Proteins