High impact information on SHE3

• She1p, which is identical to the minimyosin Myo4p, and She3p are not, however, mother-specific proteins [1].
• These mRNAs associate with Myo4p via the She2p and She3p proteins [2].
• She2p can interact with She3 protein via She3p's C-terminus and becomes localized to the daughter cell tip upon ASH1 expression [3].
• The N-terminal coiled-coil domain of She3p is required to form an RNA-independent complex with the heavy chain of the myosin motor protein Myo4p [3].

Biological context of SHE3

• By tethering a She3p-MS2 fusion protein to a reporter RNA containing MS2 binding sites, we observed that She2p is dispensable for She3p-MS2-dependent RNA localization [4].
• In yeast, mRNA localization to the growing bud depends on the myosin Myo4p, its adaptor She3p, and the specific RNA binding protein She2p [5].

Anatomical context of SHE3

• Subcellular fractionation experiments demonstrate a cosegregation of ER and She2p, which is independent of Myo4p, She3p, or polysomes [5].

Other interactions of SHE3

• She2p and She3p are the first examples of adapters for tethering a localized mRNA to the motor protein and might serve as prototypes for RNA-motor protein adapters [3].

References