High impact information on SHE2

• Formation of the ASH1 mRNP requires recognition of zip code elements by the RNA binding protein She2p [1].
• She2p is a novel RNA binding protein with a basic helical hairpin motif [1].
• These mRNAs associate with Myo4p via the She2p and She3p proteins [2].
• Consistently, inhibition of nuclear mRNA export results in nuclear accumulation of She2p and cytoplasmic Myo4p mislocalization [3].
• Bud-specific enrichment depends on Myo4p's association with its cargo, a ribonucleoprotein complex containing the RNA-binding protein She2p [3].

Biological context of SHE2

• 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].
• To identify additional localized mRNAs, we immunoprecipitated the RNA transport components She2p, She3p, and Myo4p and performed DNA microarray analysis of their associated RNAs [5].

Anatomical context of SHE2

• Subcellular fractionation experiments demonstrate a cosegregation of ER and She2p, which is independent of Myo4p, She3p, or polysomes [6].

Physical interactions of SHE2

• Here we show that She2p is a novel RNA-binding protein that binds specifically to ASH1 mRNA in vivo and to ASH1 RNA zip codes in vitro [7].
• These mutants are defective for RNA-binding activity but retain the ability to interact with She3p, indicating that a functional She2p RNA-binding domain is not a prerequisite for association with She3p [8].

Other interactions of SHE2

• A mutant She2 protein that is unable to recognize its cognate target mRNA, ASH1, fails to localize Myo4p [3].
• 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 [7].
• In yeast, mRNA localization to the growing bud depends on the myosin Myo4p, its adaptor She3p, and the specific RNA binding protein She2p [6].

References