Probing region-resolved heterogeneity of phosphoproteome in human lens by hybrid metal organic frameworks

Phosphorylation plays crucial parts in lenticular biological function. Getting knowledge of region-resolved phosphoproteome contributes to better comprehending the pathogenesis. Here, we prepared the hybrid metal organic frameworks (HMOFs) for probing the region-resolved heterogeneity of phosphoproteome in human lens. 1334 phosphosites corresponding to 564 phosphoproteins, 1160 phosphosites corresponding to 316 phosphoproteins and 517 phosphosites corresponding to 205 phosphoproteins were identified in capsule, cortex and nucleus, respectively, providing the relatively extensive distribution mapping of phosphorylation in human lens for the first time. The label-free quantification experiments and principal component analysis presented differential expression of phopshoproteins in three subregions. For instance, & alpha;-crystallin, & beta;-crystallin and fibrillin-1 closely associated with cataract and Marfan syndrome showed disparate spatial distribution. The preferential phosphoproteins in capsule, cortex and nucleus were involved in cytoskeleton organization, metabolic process and lens development in camera-type eye, respectively. This work first provided a general overview of region-resolved phosphoproteome of human lens.