Zheng et al. (Abstract 516) described the characterization of PAT1, a novel protein that binds to an 11-residue segment of the amyloid precursor protein (APP) in yeast 2-hybrid assays. PAT1 also bind to microtubules (MT). When coexpressed in HeLa and MDCK cells, PAT1 and APP partially co-localize by double immunofluorescence microscopy. The two proteins also cofractionate in sucrose gradients. The authors suggest that PAT1 is involved in sorting or trafficking of APP since heterologous expression of a HAT reporter fused to a segment of APP is differentially modulated when coexpressed with PAT1. Thus HAT activity increased when PAT1 was coexpressed in its sense orientation, but decreased when PAT was expressed in its anti-sense orientation.—June Kinoshita


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