Disease relevance of RCY1

• Of three mutants examined (vps45, vma3, and rcy1), all were found to have defective calcium homeostasis, supporting a correlation with amiodarone hypersensitivity [1].

High impact information on RCY1

• Mutation of RCY1 leads to the accumulation of an enlarged compartment that contains the t-SNARE Tlg1p and lies close to areas of cell expansion [2].
• Deletion of RCY1 leads to an early block in the endocytic pathway before the intersection with the vacuolar protein sorting pathway [2].
• Importantly, Skp1p was the only major partner that copurified with Rcy1p [3].
• Rcy1p localized to areas of polarized growth, and this polarized localization required its CAAX box and an intact actin cytoskeleton [3].
• Unlike the case for F-box proteins that are known to participate in SCF complexes, degradation of Rcy1p required neither its F box nor functional 26S proteasomes or other SCF core subunits [3].

Biological context of RCY1

• We show that like Rcy1, Ypt31/32 regulate the coupled phosphorylation and recycling of the plasma membrane v-SNARE Snc1 [4].

Physical interactions of RCY1

• In addition, Rcy1p coimmunoprecipitated with Cdc50p-Drs2p [5].
• Finally, we show that Rcy1 physically interacts with Snc1 [4].

Regulatory relationships of RCY1

• Furthermore, Ypt31/32 regulates the polarized localization and half-life of Rcy1 [4].
• Moreover, Ypt31/32 and Rcy1 regulate the recycling of the furin-homolog Kex2 to the Golgi [4].

Other interactions of RCY1

• Three of these genes were identified on the basis of trafficking defects by ourselves and others within the EUROFAN project (TLG2, RCY1, MON2) [6].
• Our results thus suggest that a complex composed of Rcy1p and Skp1p but not other SCF components may play a direct role in recycling of internalized proteins [3].

References