Medical Journals

Sara-regulated Vesicular Targeting Underlies Formation of the Light-sensing Organelle in Mammalian Rods.

Authors:
  • Chuang Jen-Zen
  • Zhao Yu
  • Sung Ching-Hwa

From: Margaret M. Dyson Vision Research Institute, Department of Ophthalmology, Weill Medical College of Cornell University, 1300 York Avenue, New York, NY 10021, USA. izchuang@med.cornell.edu

Cell

  • Publish Date: Aug 2007
  • ISSN: 0092-8674
  • Volume: 130
  • Issue: 3
  • Pages: 535-47
  • Medium: Print
  • Language: English
  • Citation (JAMA): Chuang Jen-Zen, Zhao Yu, Sung Ching-Hwa, et al. Sara-regulated Vesicular Targeting Underlies Formation of the Light-sensing Organelle in Mammalian Rods.. Cell Aug 2007;130:535-47

Abstract

The light-sensing organelle of the vertebrate rod photoreceptor, the outer segment (OS), is a modified cilium containing approximately 1,000 stacked disc membranes that are densely packed with visual pigment rhodopsin. The mammalian OS is renewed every ten days; new discs are assembled at the base of the OS by a poorly understood mechanism. Our results suggest that discs are formed and matured in a process that involves specific phospholipid-directed vesicular membrane targeting. Rhodopsin-laden vesicles in the OS axonemal cytoplasm fuse with nascent discs that are highly specialized with abundant phosphatidylinositol 3-phosphate (PI3P). This membrane coupling is regulated by the FYVE domain-containing protein, SARA, through its direct interaction with PI3P, rhodopsin, and SNARE protein syntaxin 3. Our model, in contrast to the previously proposed evagination model, suggests that the vesicular delivery of rhodopsin in the OS concentrates rhodopsin into discs, and this process directly participates in disc biogenesis.

Mesh Headings (Keywords): Animals, Animals, Genetically Modified, Animals, Newborn, Cell Differentiation, Cell Line, Cytoplasmic Vesicles, Humans, Intracellular Signaling Peptides and Proteins, Light, Mice, Organelles, Peptide Fragments, Rats, Rhodopsin, Rod Outer Segments, Serine Endopeptidases


Check for Full Text / PubMed Unique Identifier (PMID): 17693260


This abstract is part of PubMed, a service of the U.S. National Library of Medicine. PubMed includes more than 17 million citations from MEDLINE and other life science journals for biomedical articles. See Copyright and Disclaimers.

Linked medical terms appearing on this page are added by Healia to help readers find more information and are not part of the original PubMed document.

The data herein was last updated on July 8th, 2008 and may not reflect the most current and accurate data available from NLM.


Advertisements

About | Privacy Policy | Business Solutions | Advertise | Contact | Add Healia to your site

©2012. Healia / Meredith Corporation  

Use of this site constitutes acceptance of our Terms of Service and Privacy Policy. All content on this Web site, including medical opinion and any other health-related information, is for informational purposes only and should not be used for a specific diagnosis or individual treatment plan for any situation. Use of this site and the information contained herein does not create a doctor-patient relationship. Always seek the direct advice of your doctor in connection with any questions or issues you may have regarding your own health or the health of others.