TY  - JOUR
AU  - Schaap, I.A.T.
AU  - Hoffmann, B.
AU  - Carrasco, C.
AU  - Merkel, R.
AU  - Schmidt, C. F.
TI  - Tau protein binding forms a 1 nm thick layer along protofilaments without affecting the radial elasticity of microtubules
JO  - Journal of structural biology
VL  - 158
SN  - 1047-8477
CY  - San Diego, Calif.
PB  - Elsevier
M1  - PreJuSER-57095
SP  - 282 - 292
PY  - 2007
N1  - Record converted from VDB: 12.11.2012
AB  - Tau is one of the most abundant microtubule-associated proteins involved in kinetic stabilization and bundling of axonal microtubules. Although intense research has revealed much about tau function and its involvement in Alzheimer's disease during the past years, it still remains unclear how exactly tau binds on microtubules and if the kinetic stabilization of microtubules by tau is accompanied, at least in part, by a mechanical reinforcement of microtubules. In this paper, we have used atomic force microscopy to address both aspects by visualizing and mechanically analyzing microtubules in the presence of native tau isoforms. We could show that tau at saturating concentrations forms a 1 nm thick layer around the microtubule, but leaves the protofilament structure well visible. The latter observation argues for tau binding mainly along and not across the protofilaments. The radial elasticity of microtubules was almost unaffected by tau, consistent with tau binding along the tops of the protofilaments. Tau did increase the resistance of microtubules against rupture. Finite-element calculations confirmed our findings.
KW  - Animals
KW  - Elasticity
KW  - Kinetics
KW  - Microscopy, Atomic Force
KW  - Microtubule-Associated Proteins: chemistry
KW  - Microtubules: chemistry
KW  - Protein Binding
KW  - Protein Isoforms
KW  - Swine: metabolism
KW  - tau Proteins: chemistry
KW  - Microtubule-Associated Proteins (NLM Chemicals)
KW  - Protein Isoforms (NLM Chemicals)
KW  - tau Proteins (NLM Chemicals)
KW  - J (WoSType)
LB  - PUB:(DE-HGF)16
C6  - pmid:17329123
UR  - <Go to ISI:>//WOS:000246927800003
DO  - DOI:10.1016/j.jsb.2006.11.010
UR  - https://juser.fz-juelich.de/record/57095
ER  -