High impact information on LSB5

• Our data demonstrate that Ysc84p and Lsb5p are important components of complexes involved in overlapping pathways coupling endocytosis with the actin cytoskeleton in yeast [1].
• Both Ysc84p and Lsb5p were identified through two-hybrid screens with different domains of the adaptor protein Sla1p [1].
• Here we demonstrate the importance of two additional cortical components, Ysc84p and Lsb5p, which together are essential for the organization of the actin cytoskeleton and for fluid phase endocytosis [1].
• We also demonstrate hitherto unknown interactions between Lsb5p and the active form of the yeast Arf3 protein, and with ubiquitin [2].
• Lsb5p has a similar structure to the GGA [Golgi-localized, gamma-ear-containing, Arf (ADP-ribosylation factor)-binding] family of proteins with an N-terminal VHS [Vps27p (vacuolar protein sorting protein 27), Hrs, Stam] domain and a GAT (GGA and Tom1) domain [2].

Biological context of LSB5

• Previously, we reported that the Lsb5 protein plays a role in endocytosis in yeast and that it localizes to the plasma membrane [2].

Other interactions of LSB5

• Interactions between Sla1p, Lsb5p and Arf3p in yeast endocytosis [3].
• Ycl034w/Lsb5p localizes to the cell cortex but does not colocalize with actin [1].

References