Skip Navigation

This Article
Right arrow Full Text (PDF)
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 Add to My Personal Archive
Right arrow Download to citation manager
Right arrowRequest Permissions
Google Scholar
Right arrow Articles by Swatzell, L. J.
Right arrow Articles by Kiss, J. Z.
Right arrow Search for Related Content
PubMed
Right arrow PubMed Citation
Right arrow Articles by Swatzell, L. J.
Right arrow Articles by Kiss, J. Z.
Agricola
Right arrow Articles by Swatzell, L. J.
Right arrow Articles by Kiss, J. Z.
Social Bookmarking
Add to CiteULike   Add to Connotea   Add to Del.icio.us  
What's this?

Plant and Cell Physiology, 1999, Vol. 40, No. 2 173-183
© 1999

Integrin-Like Proteins are Localized to Plasma Membrane Fractions, not Plastids, in Arabidopsis

Lucinda J. Swatzell1, Richard E. Edelmann1, Christopher A. Makaroff2 and John Z. Kiss1,3

1 Department of Botany, Miami University Oxford OH, 45056, U.S.A.
2 Department of Chemistry and Biochemistry, Miami University Oxford OH, 45056, U.S.A.

3 kissjz{at}muohio.edu

Integrins are a large family of integral membrane proteins that function in signal transduction in animal systems. These proteins are conserved in vertebrates, invertebrates, and fungi. Evidence from previous research suggests that integrin-like proteins may be present in plants as well, and that these proteins may function in signal transduction during gravitropism. In past studies, researchers have used monoclonal and polyclonal antibodies to localize ß1 integrin-like proteins in plants. However, there is a disparity between data collected from these studies, especially since molecular weights obtained from these investigations range from 55–120 kDa for integrin-like proteins. To date, a complete investigation which employs all three basic immunolabeling procedures, immunoblotting, immunofluorescence microscopy, and immunogold labeling, in addition to extensive fractionation and exhaustive controls, has been lacking. In this paper, we demonstrate that use of a polyclonal antibody against the cytoplasmic domain of avian ß1-integrin can produce potential artifacts in immunolocalization studies. However, these problems can be eliminated through use of starchless mutants or proper specimen preparation prior to electrophoresis. We also show that this antibody, when applied within the described parameters and with careful controls, identifies a large (100 kDa) integrin-like protein that is localized to plasma membrane fractions in Arabidopsis.

(Received October 5, 1998; Accepted November 26, 1998)
Add to CiteULike CiteULike   Add to Connotea Connotea   Add to Del.icio.us Del.icio.us    What's this?


This article has been cited by other articles:


Home page
 Plant CellHome page
V. A. Manning and L. M. Ciuffetti
Localization of Ptr ToxA Produced by Pyrenophora tritici-repentis Reveals Protein Import into Wheat Mesophyll Cells
PLANT CELL, November 1, 2005; 17(11): 3203 - 3212.
[Abstract] [Full Text] [PDF]

Home page
 Plant Physiol.Home page
F. Baluska, J. Samaj, P. Wojtaszek, D. Volkmann, and D. Menzel
Cytoskeleton-Plasma Membrane-Cell Wall Continuum in Plants. Emerging Links Revisited
Plant Physiology, October 1, 2003; 133(2): 482 - 491.
[Full Text] [PDF]


Disclaimer: Please note that abstracts for content published before 1996 were created through digital scanning and may therefore not exactly replicate the text of the original print issues. All efforts have been made to ensure accuracy, but the Publisher will not be held responsible for any remaining inaccuracies. If you require any further clarification, please contact our Customer Services Department.