Does vAPB/ALS8 interact with FFAT-like proteins including the p97 cofactor FAF1 and the ASNA1 ATPase?
The FFAT-like motifs we identified in FAF1 and ASNA1 demonstrate that sequences containing a single phenylalanine residue with the consensus (D/E)(D/E)FEDAx(D/E) are also proficient to mediate interaction with VAPB. Our findings indicate that the repertoire of VAPB interactors is more diverse than previously anticipated and link VAPB to the function of ATPase complexes such as p97/FAF1 and ASNA1/TRC.
Apoptotic epithelial cells and BP were significantly increased in the CF group and excess level of apoptosis may be the result of enhanced occurrence of BP. Apoptotic cells were alveolar epithelial cells in the great majority of the patients and were not detected in other locations where CFTR expression is much more prominent than alveolar cells. We may postulate that increased apoptotic findings in the alveolar epithelium were related with the presence of chronic infections rather than CFTR dysfunction.