spacer gif spacer gif spacer gif spacer gif spacer gif
QUICK SEARCH:   [advanced]


spacer gif
     Home     Help     Feedback     Subscriptions     Archive     Search    

The fully linked HTML version of this article has now been published.
JCS ePress online publication date 2 Nov 2004
doi: 10.1242/jcs.01512

This Article
Right arrow Full Text (PDF)
Right arrow All Versions of this Article:
jcs.01512v1
117/24/5825    most recent
Right arrow Alert me when this article is cited
Right arrow Alert me if a correction is posted
Services
Right arrow Email this article to a friend
Right arrow Similar articles in this journal
Right arrow Similar articles in PubMed
Right arrow Alert me to new issues of the journal
Right arrow Download to citation manager
Right arrow reprints & permissions
Citing Articles
Right arrow Citing Articles via HighWire
Right arrow Citing Articles via Google Scholar
Google Scholar
Right arrow Articles by Lin-Jones, J.
Right arrow Articles by Burnside, B.
Right arrow Search for Related Content
PubMed
Right arrow PubMed Citation
Right arrow Articles by Lin-Jones, J.
Right arrow Articles by Burnside, B.

Research Article

Myosin 3A transgene expression produces abnormal actin filament bundles in transgenic Xenopus laevis rod photoreceptors


Jennifer Lin-Jones*, Ed Parker, Mike Wu, Andréa Dosé, and Beth Burnside
* Author for correspondence (e-mail: linjones{at}berkeley.edu)

Myo3A, a class III myosin, localizes to the distal (plus) ends of inner segment actin filament bundles that form the core of microvillus-like calycal processes encircling the base of the photoreceptor outer segment. To investigate Myo3A localization and function, we expressed green fluorescent protein-tagged bass Myo3A and related constructs in transgenic Xenopus rods using a modified opsin promoter. Tagged intact Myo3A localized to rod calycal processes, as previously reported for native bass Myo3A. Transgenic rods developed abnormally large calycal processes and subsequently degenerated. Modified Myo3A expression constructs demonstrated that calycal process localization required an active motor domain and the tail domain. Expressed tail domain alone localized to actin bundles along the entire inner segment length, rather than to the distal end. This tail domain localization required the conserved C-terminal domain (3THDII) previously shown to possess an actin-binding motif. Our findings suggest that Myo3A plays a role in the morphogenesis and maintenance of calycal processes of vertebrate photoreceptors.


This article has been cited by other articles:


Home page
 IOVSHome page
J. Lin-Jones and B. Burnside
Retina-Specific Protein Fascin 2 Is an Actin Cross-linker Associated with Actin Bundles in Photoreceptor Inner Segments and Calycal Processes
Invest. Ophthalmol. Vis. Sci., March 1, 2007; 48(3): 1380 - 1388.
[Abstract] [Full Text] [PDF]

Home page
 J. Biol. Chem.Home page
A. C. Dose, S. Ananthanarayanan, J. E. Moore, B. Burnside, and C. M. Yengo
Kinetic Mechanism of Human Myosin IIIA
J. Biol. Chem., January 5, 2007; 282(1): 216 - 231.
[Abstract] [Full Text] [PDF]

Home page
 J. Biol. Chem.Home page
T. Kambara, S. Komaba, and M. Ikebe
Human Myosin III Is a Motor Having an Extremely High Affinity for Actin
J. Biol. Chem., December 8, 2006; 281(49): 37291 - 37301.
[Abstract] [Full Text] [PDF]

Home page
 J. Neurosci.Home page
M. E. Schneider, A. C. Dose, F. T. Salles, W. Chang, F. L. Erickson, B. Burnside, and B. Kachar
A New Compartment at Stereocilia Tips Defined by Spatial and Temporal Patterns of Myosin IIIa Expression
J. Neurosci., October 4, 2006; 26(40): 10243 - 10252.
[Abstract] [Full Text] [PDF]


© The Company of Biologists Ltd 2004