The canonical role of glyceraldehyde phosphate dehydrogenase (GAPDH) is as an enzyme in glycolysis. GAPDH is also a principal "moonlighting" protein with additional roles at diverse sites in a variety of cells. Surface GAPDH on mammalian， yeast， and bacterial cells acts as a receptor and also mediates cell contacts. In neurons， extracellular GAPDH localizes at synapses. Two GAPDH binding partners at synapses are α-Amino-3-hydroxy-5-methyl-4-isoxazolepropionic acid glutamate receptor (AMPA) GluA2 subunit at dendritic spines and L1 cell adhesion molecule at pre-synaptic membranes， and both proteins are also expressed in lenses. Fiber cell membrane protrusions and dendritic spines have similar size， shape， and spacing， contain F-actin， and express clathrin/AP-2 Adaptor at their surfaces linked with Tyr-phosphatase STEP-regulated endocytosis of AMPA/GluA2 receptors. AMPA receptors work with NMDA (N-methyl-d-aspartate) and GABA (γ-aminobutyric acid) receptors， calcium calmodulin kinase II (CaMKIIα)， channel proteins， STEP， and ephrin receptors， which are also expressed in lenses. In neurons， coordinate AMPA/GluA2 receptor endocytosis with GAPDH is linked with disease. GAPDH was previously characterized as a fiber cell membrane protein and shown to decrease substantially in interior fiber cells in human age-related cataract. Here， we examined GAPDH spatial expression in healthy lenses in two vertebrate species.