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Lack of protein‐tyrosine sulfation disrupts photoreceptor outer segment morphogenesis, retinal function and retinal anatomy
Author(s) -
Sherry David M.,
Murray Anne R.,
Kanan Yogita,
Arbogast Kelsey L.,
Hamilton Robert A.,
Fliesler Steven J.,
Burns Marie E.,
Moore Kevin L.,
AlUbaidi Muayyad R.
Publication year - 2010
Publication title -
european journal of neuroscience
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 1.346
H-Index - 206
eISSN - 1460-9568
pISSN - 0953-816X
DOI - 10.1111/j.1460-9568.2010.07431.x
Subject(s) - retina , retinal , morphogenesis , biology , microbiology and biotechnology , sulfation , anatomy , neuroscience , biochemistry , gene
To investigate the role(s) of protein‐tyrosine sulfation in the retina, we examined retinal function and structure in mice lacking tyrosylprotein sulfotransferases (TPST) 1 and 2. Tpst double knockout (DKO; Tpst1 −/− /Tpst2 −/− ) retinas had drastically reduced electroretinographic responses, although their photoreceptors exhibited normal responses in single cell recordings. These retinas appeared normal histologically; however, the rod photoreceptors had ultrastructurally abnormal outer segments, with membrane evulsions into the extracellular space, irregular disc membrane spacing and expanded intradiscal space. Photoreceptor synaptic terminals were disorganized in Tpst DKO retinas, but established ultrastructurally normal synapses, as did bipolar and amacrine cells; however, the morphology and organization of neuronal processes in the inner retina were abnormal. These results indicate that protein‐tyrosine sulfation is essential for proper outer segment morphogenesis and synaptic function, but is not critical for overall retinal structure or synapse formation, and may serve broader functions in neuronal development and maintenance.