Vrp1p (yeast WIP) forms a protein complex with Las17p (yeast WASP), however the physiological significance of the interaction has not been fully characterized. Vrp1p residues, 788 MPKPR 792 are essential for Vrp1p–Las17p interaction. While C-Vrp1p 364–817 complements all the defects of the vrp1Δ strain, C-Vrp1p 364–817 5A ( 788 AAAAA 792 ) does not complement any of the defects, due to its inability to localize to cortical patches. Targeting C-Vrp1p 364–817 5A to membranes using CAAX motif (C-Vrp1p 364–817 5A -CAAX) rescued the growth and endocytosis defect but not the actin patch polarization defect of vrp1Δ. Vrp1p can localize to cortical patches, either by binding to Las17p through LBD (Las17 Binding Domain, Vrp1p 760–817 ) or independent of Las17p through residues in N-Vrp1p 1–364 . Unlike Vrp1p, Vrp1p 5A localizes poorly to cortical patches and complements all the defects of vrp1Δ strain except actin patch polarization at elevated temperature. N-Vrp1p 1–364 complements all the defects of vrp1Δ strain except the actin patch polarization defect while N-Vrp1p 1–364 –LBD fusion protein complements all the defects. Thus our results show that while both Vrp1p and Las17p are essential for many cellular processes, the two proteins do not necessarily have to bind to each other to carry out these cellular functions. However, Las17p–Vrp1p interaction is essential for actin patch polarization at elevated temperature.