Psychiatry related information on SMY1

• Furthermore, a mutation in SMY1 strongly predicted to destroy motor activity does not destroy Smy1p function [1].

High impact information on SMY1

• We have also observed a genetic interaction between SMY1 and two of the late SEC mutations, sec2 and sec4 [1].
• Unexpectedly, we found that abolition of microtubules by nocodazole does not interfere with the ability of Smy1p to correct the mutant Myo2p defect, nor does it interfere with the ability of Smy1p to localize properly [1].
• We have previously reported that a defect in Myo2p, a myosin in budding yeast (Saccharomyces cerevisiae), can be partially corrected by overexpression of Smy1p, which is by sequence a kinesin-related protein (Lillie, S.H., and S.S. Brown. 1992. Nature. 356:358- 361) [1].
• Such a functional link between putative actin- and microtubule-based motors is surprising, so here we have tested the prediction that Smy1p indeed acts as a microtubule-based motor [1].
• Smy1p, a kinesin-related protein that does not require microtubules [1].

Biological context of SMY1

• The rearrangements of Myo2p and Smy1p correlate temporally with those of actin spots during the cell cycle, and upon temperature and osmotic shift [2].
• Sequence analysis of a 10 kb fragment of yeast chromosome XI identifies the SMY1 locus and reveals sequences related to a pre-mRNA splicing factor and vacuolar ATPase subunit C plus a number of unidentified open reading frames [3].

Physical interactions of SMY1

• We now show by two-hybrid analysis that a 69-amino acid region of the Smy1p tail interacts with the globular portion of the Myo2p tail [4].

Regulatory relationships of SMY1

• We propose that Smy1p enhances some aspect of Myo2p function, perhaps delivery or docking of vesicles at the bud tip [4].

Other interactions of SMY1

• However, the lethality of MYO2 deletion is not overcome by SMY1 overexpression [2].
• Bnr1p, but not Bni1p, directly interacted with the C-terminal region of Smy1p [5].
• The yeast kinesin-related protein Smy1p exerts its effects on the class V myosin Myo2p via a physical interaction [4].

Analytical, diagnostic and therapeutic context of SMY1

• Immunofluorescence localization of the unconventional myosin, Myo2p, and the putative kinesin-related protein, Smy1p, to the same regions of polarized growth in Saccharomyces cerevisiae [2].

References