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 arrow Request Permissions
Google Scholar
Right arrow Articles by Nakamura, A.
Right arrow Articles by Fujii, T.
Right arrow Search for Related Content
PubMed
Right arrow PubMed Citation
Right arrow Articles by Nakamura, A.
Right arrow Articles by Fujii, T.
Social Bookmarking
Add to CiteULike   Add to Connotea   Add to Del.icio.us  
What's this?

J. Biochem, 1989, Vol. 106, No. 1 93-97
© 1989 Japanese Biochemical Society

research-article

Inhibitory Effects of Poly(L-Aspartic Acid) on the Assembly of Brain Microtubules and the Interaction of Microtubule-Associated Protein 2 with F-Actin In Vitro

Akira Nakamura*, Takao Arai**, Yoshiyuki Kondo* and Toshihiro Fujii*,1

*Department of Functional Polymer Science, Faculty of Textile Science and Technology, Shinshu University Veda, Nagano 386
**Institute of Basic Medical Sciences, University of Tsukuba Tsukuba, Ibaraki 305

1To whom correspondence should be addressed

The effects of poly(L-aspartic acid) (PLAA) on microtubule assembly and microtubule-associated protein (MAP) 2-actin interaction were examined in vitro. PLAA inhibited assembly of rat brain microtubules and induced rapid disassembly of already formed microtubules. Inhibition was stronger by PLAA with a high molecular weight than that by low molecular weight. The ratios of 47 kDa PLAA to microtubule proteins causing 50% inhibition of the assembly and disassembly were 0.015 and 0.04 (w/w), respectively. Both MAP 1 and MAP 2 were bound to a PLAA-Sepharose 4B affinity column, while tubulin was not retained by the column. PLAA caused selective dissociation of MAP 1 and MAP 2 from microtubules polymerized by taxol. It is therefore concluded that PLAA interacts specifically with MAPs. PLAA also inhibited the MAP 2 induced cross-linking of actin filaments, showing an almost complete inhibition at a PLAA to MAP 2 ratio of 1: 5, 000 (w/w). Binding experiments of PLAA with digested MAP 2 by chymotrypsin using affinity chromatography and sedimentation experiments showed that PLAA was preferentially bound to a 35 kDa fragment which includes the microtubule- and actin-binding domain of the MAP 2 molecule. These results suggest that PLAA suppressed the functions of MAP 2 through a domain which is located in the 35 kDa fragment.


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
 Mol. Biol. CellHome page
S. Timm, B. Titus, K. Bernd, and M. Barroso
The EF-hand Ca2+-binding Protein p22 Associates with Microtubules in an N-Myristoylation-dependent Manner
Mol. Biol. Cell, October 1, 1999; 10(10): 3473 - 3488.
[Abstract] [Full Text]


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.