Molecular Biology of the Cell click for CBE Life Science Education Page

Home Help [Feedback] [For Subscribers] [Archive] [Search] [Contents]
QUICK SEARCH:   [advanced]


     

Originally published as MBC in Press, 10.1091/mbc.E07-03-0278 on August 29, 2007

Vol. 18, Issue 11, 4317-4326, November 2007

This Article
Right arrow Full Text
Right arrow Full Text (PDF)
Right arrow All Versions of this Article:
E07-03-0278v1
18/11/4317    most recent
Right arrow Alert me when this article is cited
Right arrow Alert me if a correction is posted
Services
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 Qadota, H.
Right arrow Articles by Benian, G. M.
Right arrow Search for Related Content
PubMed
Right arrow PubMed Citation
Right arrow Articles by Qadota, H.
Right arrow Articles by Benian, G. M.

Two LIM Domain Proteins and UNC-96 Link UNC-97/PINCH to Myosin Thick Filaments in Caenorhabditis elegans Muscle

Hiroshi Qadota*, Kristina B. Mercer*, Rachel K. Miller*, Kozo Kaibuchi{dagger}, and Guy M. Benian*

*Department of Pathology, Emory University, Atlanta, GA 30322; and {dagger}Department of Cell Pharmacology, Nagoya University, Graduate School of Medicine, Aichi 466-8550, Japan

Submitted March 27, 2007; Revised August 10, 2007; Accepted August 20, 2007
Monitoring Editor: Erika Holzbaur

By yeast two-hybrid screening, we found three novel interactors (UNC-95, LIM-8, and LIM-9) for UNC-97/PINCH in Caenorhabditis elegans. All three proteins contain LIM domains that are required for binding. Among the three interactors, LIM-8 and LIM-9 also bind to UNC-96, a component of sarcomeric M-lines. UNC-96 and LIM-8 also bind to the C-terminal portion of a myosin heavy chain (MHC), MHC A, which resides in the middle of thick filaments in the proximity of M-lines. All interactions identified by yeast two-hybrid assays were confirmed by in vitro binding assays using purified proteins. All three novel UNC-97 interactors are expressed in body wall muscle and by antibodies localize to M-lines. Either a decreased or an increased dosage of UNC-96 results in disorganization of thick filaments. Our previous studies showed that UNC-98, a C2H2 Zn finger protein, acts as a linkage between UNC-97, an integrin-associated protein, and MHC A in myosin thick filaments. In this study, we demonstrate another mechanism by which this linkage occurs: from UNC-97 through LIM-8 or LIM-9/UNC-96 to myosin.

This was published online ahead of print in MBC in Press (http://www.molbiolcell.org/cgi/doi/10.1091/mbc.E07-03-0278) on August 29, 2007.

Address correspondence to: Guy M. Benian (pathgb{at}emory.edu)




This article has been cited by other articles:


Home page
 Mol. Biol. CellHome page
H. Qadota, L. A. McGaha, K. B. Mercer, T. J. Stark, T. M. Ferrara, and G. M. Benian
A Novel Protein Phosphatase is a Binding Partner for the Protein Kinase Domains of UNC-89 (Obscurin) in Caenorhabditis elegans
Mol. Biol. Cell, June 1, 2008; 19(6): 2424 - 2432.
[Abstract] [Full Text] [PDF]

Home page
 Mol. Biol. CellHome page
R. K. Miller, H. Qadota, K. B. Mercer, K. M. Gernert, and G. M. Benian
UNC-98 and UNC-96 Interact with Paramyosin to Promote Its Incorporation into Thick Filaments of Caenorhabditis elegans
Mol. Biol. Cell, April 1, 2008; 19(4): 1529 - 1539.
[Abstract] [Full Text] [PDF]


Home Help [Feedback] [For Subscribers] [Archive] [Search] [Contents]
Copyright © 2007 by The American Society for Cell Biology. Terms of copyright protection, warranties, and disclaimers.