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The yeast N-BAR (Bin/Amphiphysin/Rvs167) protein Rvs167 is recruited by the Rab  G TPase  A ctivating  P roteins (RabGAP) Gyp5 and Gyl1 to the tip of small buds to act in exocytosis. Investigating other N-BAR proteins involved in Gyp5/Gyl1/Rvs167 complexes, we found that Rvs161, an Rvs167 paralog, is absent from the complexes formed at the tip of small buds. Immunoprecipitation and  B imolecular  F luorescence  C omplementation (BiFC) analysis show that both Rvs167 and Rvs161 interact  in vivo  with Gvp36, an N-BAR protein. Rvs167 molecules also interact independently of Rvs161 and Gvp36. Rvs167/Rvs167 and Rvs167/Gyp5 interactions predominate over other combinations at the tip of small buds, suggesting that N-BAR lattices enriched in Rvs167 molecules form at these sites. By combining BiFC with markers specific to each organelle, we analyzed systematically in living cells the locations of the BiFC signals generated by combinations of the three N-BAR proteins. We show that the BiFC signals differ according to organelle and cell site, strongly suggesting heterogeneity in the composition of N-BAR protein lattices  in vivo . Our results reveal that the organization of N-BAR protein lattices  in vivo  is complex and are consistent with N-BAR proteins forming various types of dimers and lattices of variable composition.

Three members of the yeast N-BAR proteins family form heterogeneous lattices in vivo and interact differentially with two RabGAP proteins