Identification of tau protein regions required for process formation in PC12 cells - PubMed (original) (raw)
. 1994 Dec:107 ( Pt 12):3403-12.
doi: 10.1242/jcs.107.12.3403.
Affiliations
- PMID: 7706394
- DOI: 10.1242/jcs.107.12.3403
Identification of tau protein regions required for process formation in PC12 cells
J G Léger et al. J Cell Sci. 1994 Dec.
Abstract
Tau is a neuronal microtubule-associated protein that is required for the development and maintenance of neuronal cell polarity. It promotes microtubule assembly in vitro and we have recently reported that a specific tau region, which spans amino acid residues 154-172 of human fetal tau, is not required for growth of existing microtubules, but is required for nucleation of new microtubules. These residues also confer stronger microtubule binding activity in 3T3 cells. The aim of this study was to investigate the functional organization of tau in relation to its role in promoting process formation in a neuronal model system. We transfected undifferentiated PC12 cells with vectors expressing tau fragments and treated the expressing cells with cytochalasin B to allow process extension. We found that deletion of amino acid residues 154-172 greatly reduced the percentage of transfected cells bearing processes compared to that of cells transfected with full-length tau or with an amino-terminally deleted tau fragment containing residues 154-172. These differences do not appear to result from a quantitative difference in protein expression, as shown by immunoblot analysis of transfected cells. We also observed that while the presence of tau fragments increases acetylation of microtubules, the pattern of acetylation in cells transfected with the fragment missing residues 154-172 is less extensive, suggesting that it does not result in the same level of stabilization as the longer tau fragments. Taxol promoted process outgrowth in cells treated with cytochalasin and restored process outgrowth to cells transfected with the tau fragment lacking this activity. Therefore, process formation involves primarily the stabilization and nucleation of microtubules. We conclude that the residues necessary for conferring microtubule nucleation activity of tau in vitro are important for process formation in vivo. It is likely that these residues influence the binding affinity and therefore the stabilization activity of tau.
Similar articles
- Transient expression of fluorescent tau proteins promotes process formation in PC12 cells: contributions of the tau C-terminus to this process.
Yu JZ, Kuret J, Rasenick MM. Yu JZ, et al. J Neurosci Res. 2002 Mar 1;67(5):625-33. doi: 10.1002/jnr.10152. J Neurosci Res. 2002. PMID: 11891775 - Expression of tau protein in non-neuronal cells: microtubule binding and stabilization.
Lee G, Rook SL. Lee G, et al. J Cell Sci. 1992 Jun;102 ( Pt 2):227-37. doi: 10.1242/jcs.102.2.227. J Cell Sci. 1992. PMID: 1400630 - Conversion of serine to aspartate imitates phosphorylation-induced changes in the structure and function of microtubule-associated protein tau.
Léger J, Kempf M, Lee G, Brandt R. Léger J, et al. J Biol Chem. 1997 Mar 28;272(13):8441-6. doi: 10.1074/jbc.272.13.8441. J Biol Chem. 1997. PMID: 9079670 - Sense and antisense transfection analysis of tau function: tau influences net microtubule assembly, neurite outgrowth and neuritic stability.
Esmaeli-Azad B, McCarty JH, Feinstein SC. Esmaeli-Azad B, et al. J Cell Sci. 1994 Apr;107 ( Pt 4):869-79. doi: 10.1242/jcs.107.4.869. J Cell Sci. 1994. PMID: 8056843
Cited by
- Presence of a carboxy-terminal pseudorepeat and disease-like pseudohyperphosphorylation critically influence tau's interaction with microtubules in axon-like processes.
Niewidok B, Igaev M, Sündermann F, Janning D, Bakota L, Brandt R. Niewidok B, et al. Mol Biol Cell. 2016 Nov 7;27(22):3537-3549. doi: 10.1091/mbc.E16-06-0402. Epub 2016 Aug 31. Mol Biol Cell. 2016. PMID: 27582388 Free PMC article. - The mitotic tensegrity guardian tau protects mammary epithelia from katanin-like1-induced aneuploidy.
Sudo H, Nakajima K. Sudo H, et al. Oncotarget. 2016 Aug 16;7(33):53712-53734. doi: 10.18632/oncotarget.10728. Oncotarget. 2016. PMID: 27447563 Free PMC article. - Tau potentiates nerve growth factor-induced mitogen-activated protein kinase signaling and neurite initiation without a requirement for microtubule binding.
Leugers CJ, Lee G. Leugers CJ, et al. J Biol Chem. 2010 Jun 18;285(25):19125-34. doi: 10.1074/jbc.M110.105387. Epub 2010 Apr 7. J Biol Chem. 2010. PMID: 20375017 Free PMC article. - Tau protects microtubules in the axon from severing by katanin.
Qiang L, Yu W, Andreadis A, Luo M, Baas PW. Qiang L, et al. J Neurosci. 2006 Mar 22;26(12):3120-9. doi: 10.1523/JNEUROSCI.5392-05.2006. J Neurosci. 2006. PMID: 16554463 Free PMC article. - Allele-specific silencing of dominant disease genes.
Miller VM, Xia H, Marrs GL, Gouvion CM, Lee G, Davidson BL, Paulson HL. Miller VM, et al. Proc Natl Acad Sci U S A. 2003 Jun 10;100(12):7195-200. doi: 10.1073/pnas.1231012100. Epub 2003 Jun 2. Proc Natl Acad Sci U S A. 2003. PMID: 12782788 Free PMC article.
Publication types
MeSH terms
Substances
LinkOut - more resources
Full Text Sources
Other Literature Sources