Publications by authors named "Anja Rac-Justament"
Article Synopsis
- Radiotherapy for prostate cancer can lead to radioresistance, which involves cell adhesion signaling and changes in the protein composition of the cell-matrix junctions in cancer cells.
- A mass spectrometry-based analysis compared radioresistant DU145 cells with their parental counterparts, revealing extensive matrix remodeling and altered protein expression, but no change in integrin levels.
- Specific proteins, particularly perlecan/HSPG2, were found to play a crucial role in modulating radioresistance, suggesting that targeting this protein might offer new therapeutic strategies for treating prostate cancer.
In vascular plants, the final photosynthetic electron transfer from ferredoxin (Fd) to NADP is catalyzed by the flavoenzyme ferredoxin:NADP oxidoreductase (FNR). FNR is recruited to thylakoid membranes via an integral membrane protein TROL (thylakoid rhodanese-like protein) and the membrane associated protein Tic62. We have previously demonstrated that the absence of TROL triggers a very efficient superoxide (O) removal mechanism.
View Article and Find Full Text PDFBackground: Focal adhesions (FAs) are integrin-containing, multi-protein structures that link intracellular actin to the extracellular matrix and trigger multiple signaling pathways that control cell proliferation, differentiation, survival and motility. Microtubules (MTs) are stabilized in the vicinity of FAs through interaction with the components of the cortical microtubule stabilizing complex (CMSC). KANK (KN motif and ankyrin repeat domains) family proteins within the CMSC, KANK1 or KANK2, bind talin within FAs and thus mediate actin-MT crosstalk.
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