ArticleExperimental eye research2015
MERTK signaling in the retinal pigment epithelium regulates the tyrosine phosphorylation of GDP dissociation inhibitor alpha from the GDI/CHM family of RAB GTPase effectors.
Article in Experimental eye research, 2015. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 11 papers.
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Who cites it
11 citing papers in PubMed, 22 citations in OpenAlex.
- Oxidative Stress and Energetic Failure: Common Features and Dissimilarities in 3 Different Mouse Models of Retinal Pigment Epithelium Phagocytosis Defects.Advances in experimental medicine and biology · 2025Article
- Unveiling Drivers of Retinal Degeneration in RCS Rats: Functional, Morphological, and Molecular Insights.International journal of molecular sciences · 2024Article
- Downregulation of MerTK in circulating T cells of patients with non-proliferative diabetic retinopathy.Frontiers in endocrinology · 2024Article
- Clearance phagocytosis by the retinal pigment epithelial during photoreceptor outer segment renewal: Molecular mechanisms and relation to retinal inflammation.Immunological reviews · 2023Review
- Spatiotemporal control of actomyosin contractility by MRCKβ signaling drives phagocytosis.The Journal of cell biology · 2022Article
- Article
- Review
- Detection and validation of novel mutations in MERTK in a simplex case of retinal degeneration using WGS and hiPSC-RPEs model.Human mutation · 2021Article
- The small GTPase RAB28 is required for phagocytosis of cone outer segments by the murine retinal pigmented epithelium.The Journal of biological chemistry · 2018Article
- Advanced molecular approaches pave the road to a clear-cut diagnosis of hereditary retinal dystrophies.Molecular vision · 2018Article
- Methods for culturing retinal pigment epithelial cells: a review of current protocols and future recommendations.Journal of tissue engineeringReview
Corrections and comments
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Authors and funding
6 authors at 1 institution in 1 country.
Funding
Abstract
Photoreceptor outer segments (OS) in the vertebrate retina undergo a process of continual renewal involving shedding of disc membranes that are cleared by phagocytic uptake into the retinal pigment epithelium (RPE). In dystrophic Royal College of Surgeons (RCS) rats, OS phagocytosis is blocked by a mutation in the gene encoding the receptor tyrosine kinase MERTK. To identify proteins tyrosine-phosphorylated downstream of MERTK in the RPE, MALDI-mass spectrometry with peptide-mass fingerprinting was used in comparative studies of RCS congenic and dystrophic rats. At times corresponding to peak phagocytic activity, the RAB GTPase effector GDP dissociation inhibitor alpha (GDI1) was found to undergo tyrosine phosphorylation only in congenic rats. In cryosections of native RPE/choroid, GDI1 colocalized with MERTK and the intracellular tyrosine-kinase SRC. In cultured RPE-J cells, and in transfected heterologous cells, MERTK stimulated SRC-mediated tyrosine phosphorylation of GDI1. In OS-fed RPE-J cells, GDI1 colocalized with MERTK and SRC on apparent phagosomes located near the apical membrane. In addition, both GDI1 and RAB5, a regulator of vesicular transport, colocalized with ingested OS. Taken together, these findings identify a novel role of MERTK signaling in membrane trafficking in the RPE that is likely to subserve mechanisms of phagosome formation.
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