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Multiple Domains In The Crumbs Homolog 2a (Crb2a) Protein Are Required For Regulating Rod Photoreceptor Size, Abigail Jensen, Ya-Chu Hsu
Multiple Domains In The Crumbs Homolog 2a (Crb2a) Protein Are Required For Regulating Rod Photoreceptor Size, Abigail Jensen, Ya-Chu Hsu
Biochemistry & Molecular Biology Department Faculty Publication Series
Background Vertebrate retinal photoreceptors are morphologically complex cells that have two apical regions, the inner segment and the outer segment. The outer segment is a modified cilium and is continuously regenerated throughout life. The molecular and cellular mechanisms that underlie vertebrate photoreceptor morphogenesis and the maintenance of the outer segment are largely unknown. The Crumbs (Crb) complex is a key regulator of apical membrane identity and size in epithelia and in Drosophila photoreceptors. Mutations in the human gene CRUMBS HOMOLOG 1 (CRB1) are associated with early and severe vision loss. Drosophila Crumbs and vertebrate Crb1 and Crumbs homolog 2 (Crb2) …
Tissue-Specific Requirements For Specific Domains In The Ferm Protein Moe/Epb4.1l5 During Early Zebrafish Development, Arne K. Christensen, Abigail Jensen
Tissue-Specific Requirements For Specific Domains In The Ferm Protein Moe/Epb4.1l5 During Early Zebrafish Development, Arne K. Christensen, Abigail Jensen
Biochemistry & Molecular Biology Department Faculty Publication Series
Background The FERM domain containing protein Mosaic Eyes (Moe) interacts with Crumbs proteins, which are important regulators of apical identity and size. In zebrafish, loss-of-function mutations in moe result in defects in brain ventricle formation, retinal pigmented epithelium and neural retinal development, pericardial edema, and tail curvature. In humans and mice, there are two major alternately spliced isoforms of the Moe orthologue, Erythrocyte Protein Band 4.1-Like 5 (Epb4.1l5), which we have named Epb4.1l5long and Epb4.1l5short, that differ after the FERM domain. Interestingly, Moe and both Epb4.1l5 isoforms have a putative C' terminal Type-I PDZ-Binding Domain (PBD). We previously showed that …