E3 ubiquitin ligase-mediated regulation of vertebrate ocular development; new insights into the function of SIAH enzymes

Warlen Pereira Piedade, Jakub K. Famulski

Research output: Contribution to journalReview articlepeer-review

5 Scopus citations

Abstract

Developmental regulation of the vertebrate visual system has been a focus of investigation for generations as understanding this critical time period has direct implications on our understanding of congenital blinding disease. The majority of studies to date have focused on transcriptional regulation mediated by morphogen gradients and signaling pathways. However, recent studies of post translational regulation during ocular development have shed light on the role of the ubiquitin proteasome system (UPS). This rather ubiquitous yet highly diverse system is well known for regulating protein function and localization as well as stability via targeting for degradation by the 26S proteasome. Work from many model organisms has recently identified UPS activity during various milestones of ocular development including retinal morphogenesis, retinal ganglion cell function as well as photoreceptor homeostasis. In particular work from flies and zebrafish has highlighted the role of the E3 ligase enzyme family, Seven in Absentia Homologue (Siah) during these events. In this review, we summarize the current understanding of UPS activity during Drosophila and vertebrate ocular development, with a major focus on recent findings correlating Siah E3 ligase activity with two major developmental stages of vertebrate ocular development, retinal morphogenesis and photoreceptor specification and survival.

Original languageEnglish
Pages (from-to)327-340
Number of pages14
JournalBiochemical Society Transactions
Volume49
Issue number1
DOIs
StatePublished - Feb 2021

Bibliographical note

Publisher Copyright:
© 2021 The Author(s). This is an open access article published by Portland Press Limited on behalf of the Biochemical Society and distributed under the Creative Commons Attribution License 4.0 (CC BY-NC-

Funding

J.K.F. is supported by an R01 award from the NEI: EY027805-01. W.P.P. was supported by Brazilian National Council for Scientific and Technological Development (CNPq) under grant number 202970/2014-0 and the Morgan Fellowship from the department of Biology, University of Kentucky.

FundersFunder number
National Eye Institute (NEI)EY027805-01
Conselho Nacional de Desenvolvimento Científico e Tecnológico202970/2014-0

    ASJC Scopus subject areas

    • Biochemistry

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