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      • Record: found
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      Phosphoinositides in Retinal Function and Disease

      review-article
      Author(s):
      Publication date (Electronic):
      Journal: Cells
      Publisher: MDPI
      Keywords: phosphoinositides, retinal lipids, membrane trafficking

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          Abstract

          Phosphatidylinositol and its phosphorylated derivatives, the phosphoinositides, play many important roles in all eukaryotic cells. These include modulation of physical properties of membranes, activation or inhibition of membrane-associated proteins, recruitment of peripheral membrane proteins that act as effectors, and control of membrane trafficking. They also serve as precursors for important second messengers, inositol (1,4,5) trisphosphate and diacylglycerol. Animal models and human diseases involving defects in phosphoinositide regulatory pathways have revealed their importance for function in the mammalian retina and retinal pigmented epithelium. New technologies for localizing, measuring and genetically manipulating them are revealing new information about their importance for the function and health of the vertebrate retina.

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          Most cited references137

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          Membrane recognition by phospholipid-binding domains.

          Mark Lemmon (2008)
          Many different globular domains bind to the surfaces of cellular membranes, or to specific phospholipid components in these membranes, and this binding is often tightly regulated. Examples include pleckstrin homology and C2 domains, which are among the largest domain families in the human proteome. Crystal structures, binding studies and analyses of subcellular localization have provided much insight into how members of this diverse group of domains bind to membranes, what features they recognize and how binding is controlled. A full appreciation of these processes is crucial for understanding how protein localization and membrane topography and trafficking are regulated in cells.
          Article 0 comments Cited 379 times – based on 0 reviews     Review now
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            Mammalian phospholipase C.

            Ganesh Kadamur, Kirstin E. Ross (2012)
            Phospholipase C (PLC) converts phosphatidylinositol 4,5-bisphosphate (PIP(2)) to inositol 1,4,5-trisphosphate (IP(3)) and diacylglycerol (DAG). DAG and IP(3) each control diverse cellular processes and are also substrates for synthesis of other important signaling molecules. PLC is thus central to many important interlocking regulatory networks. Mammals express six families of PLCs, each with both unique and overlapping controls over expression and subcellular distribution. Each PLC also responds acutely to its own spectrum of activators that includes heterotrimeric G protein subunits, protein tyrosine kinases, small G proteins, Ca(2+), and phospholipids. Mammalian PLCs are autoinhibited by a region in the catalytic TIM barrel domain that is the target of much of their acute regulation. In combination, the PLCs act as a signaling nexus that integrates numerous signaling inputs, critically governs PIP(2) levels, and regulates production of important second messengers to determine cell behavior over the millisecond to hour timescale.
            Article 0 comments Cited 155 times – based on 0 reviews     Review now
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              Trafficking to the ciliary membrane: how to get across the periciliary diffusion barrier?

              Maxence V. Nachury, Shao-Hua Jin, E. Seeley (2009)
              The primary cilium organizes numerous signal transduction cascades, and an understanding of signaling receptor trafficking to cilia is now emerging. A defining feature of cilia is the periciliary diffusion barrier that separates the ciliary and plasma membranes. Although lateral transport through this barrier may take place, polarized exocytosis to the base of the cilium has been the prevailing model for delivering membrane proteins to cilia. Key players for this polarized exocytosis model include the GTPases Rab8 and Rab11, the exocyst, and possibly the intraflagellar tranport machinery. In turn, the sorting of membrane proteins to cilia critically relies on the recognition of ciliary targeting signals by sorting machines such as the BBSome coat complex or the GTPase Arf4. Finally, some proteins need to exit from cilia, and ubiquitination may regulate this step. The stage is now set to dissect the interplay between signaling and regulated trafficking to and from cilia.
              Article 0 comments Cited 151 times – based on 0 reviews     Review now
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                Author and article information

                Journal
                Journal ID (nlm-ta): Cells
                Journal ID (iso-abbrev): Cells
                Journal ID (publisher-id): cells
                Title: Cells
                Publisher: MDPI
                ISSN (Electronic): 2073-4409
                Publication date (Electronic): 02 April 2020
                Publication date Collection: April 2020
                Volume: 9
                Issue: 4
                Electronic Location Identifier: 866
                Affiliations
                Verna and Marrs McLean Department of Biochemistry and Molecular Biology, Baylor College of Medicine, Houston, TX 77030, USA; twensel@ 123456bcm.edu
                Author information
                https://orcid.org/0000-0003-3518-9352
                Article
                Publisher ID: cells-09-00866
                DOI: 10.3390/cells9040866
                PMC ID: 7226789
                PubMed ID: 32252387
                SO-VID: 6b303313-4701-4e7e-8ea8-053446c29797
                Copyright © © 2020 by the author.
                License:

                Licensee MDPI, Basel, Switzerland. This article is an open access article distributed under the terms and conditions of the Creative Commons Attribution (CC BY) license ( http://creativecommons.org/licenses/by/4.0/).

                History
                Date received : 01 March 2020
                Date accepted : 30 March 2020
                Categories
                Subject: Review

                Keywords: phosphoinositides,retinal lipids,membrane trafficking
                Data availability:
                Keywords: phosphoinositides, retinal lipids, membrane trafficking

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