High impact information on SHE4

• The CRO1 protein exhibits significant similarity to the SHE4 protein, which is required for asymmetric mating-type switching in budding yeast cells [1].
• CRO1 and She4p are fungal proteins required for the segregation of other molecules in budding, endocytosis, and septation [2].
• The UNC-45 protein is predicted to contain an NH2-terminal domain with three tetratricopeptide repeat motifs, a unique central region, and a COOH-terminal domain homologous to CRO1 and She4p [2].
• This new screening strategy demonstrates a role for She4p and Pan1p in endocytosis, and provides a new general method for the identification of additional endocytosis mutants [3].
• In a variety of organisms, a novel group of proteins forming the UCS (UNC-45/CRO1/SHE4) domain-containing family are essential for proper myosin function [4].

Biological context of SHE4

• All of the amino acid substitutions caused by these mutations, V164I, N168I, N209S, and K377M, could suppress the defects of endocytosis and actin polarization of the she4/dim1 mutant as well [5].
• CONCLUSIONS: Our results suggest that She4p is a novel myosin motor domain binding protein and operates as a localized regulator of myosin function of class I and likely class V myosins [4].

Physical interactions of SHE4

• The UCS domain protein She4p binds to myosin motor domains and is essential for class I and class V myosin function [4].

Regulatory relationships of SHE4

• In vitro, She4p stimulates binding of Myo5p to filamentous actin [4].

Other interactions of SHE4

• Two-hybrid and biochemical experiments showed that She4p/Dim1p interacts with the motor domain of Myo3/5p through its UCS domain [5].
• Our results suggest that She4p/Dim1p is required for structural integrity or regulation of the motor domain of unconventional myosins [5].

References