“…Fab1 also possesses a conserved FYVE domain (Fab1, YGL023, Vps27, and EEA1) ( Figure 9) in its NH 2 -terminal part, which serves as a PtdIns [3]P-specific binding motif [123]. Moreover, Fab1 contains another conserved region central in its primary sequence (Figure 9), which shares significant homology to a motif present in a subunit of the chaperonin containing T-complex, CCT-1 [330][331][332]. CCT-1 is an eight subunit chaperone with actin and tubulin-binding specificity that shares notable similarity with the GroEL chaperonin of E. coli [333,334].…”