Table 1.

Changes in microtubules in Parkinson’s disease and other tauopathies

Disease	Changes	Mechanism/consequence	Model	Reference
Parkinson’s disease	The presence of tubulin and microtubule associated proteins in Lewy’s Bodies	Lewy bodies contain tubulin which becomes unfunctional in such a form	Human	Galloway et al. (1988)
Parkinson’s disease	Appearance of specific inclusions affecting microtubules	Dysfunction of microtubules due to formation of inclusions as response to an increase in the level of abnormal proteins in neurons	Human	Puig et al. (2005)
Parkinson’s disease	Aggregation of gamma-tubulin; destabilization of microtubules, disruption of mitotic spindles and changes in the Golgi apparatus	Gamma-globulin aggregation in the centrosome promotes the formation of inclusions, and the compound itself, affecting the structure and function of the centrosome	Primary mesencephalic cell cultures, rats	Diaz-Corrales et al. (2005)
Parkinson’s disease	Aggregation of a synuclein and tubulin	The microtubule system is a potential target for a synuclein and alterations within it can lead to disorders	SH-SY5Y human neuroblastoma cells	Lee et al. (2006)
Parkinson’s disease	Changes in expression of genes coding for ATP synthase, β IIA- tubulin, and various enzymes	Increased susceptibility to the disease	Mice	Zempel et al. (2015)
Guam ALS/parkinsonism-dementia and Down syndrome	Neurofibrillary tangles appearance which affect microtubules	Involvement of tubulin in neurofibrillary tangle formation, which in turn cause destabilization of microtubules	Human	Schwab and McGeer (1998)
Frontotemporal dementia and Parkinsonism associated with chromosome 17	Changes in the cytoskeleton related to tau-mediated changes in the number and morphology of lysosomes	Lysosomal abnormalities may contribute to cytoskeleton dysfunctions and neurodegeneration	Mice	Lim et al. (2001)
Alzheimer’s disease and frontotemporal dementia and Parkinsonism associated with chromosome 17	Abnormal microtubule morphology	Modification of tubulin may lead to intermediate or late stages in the pathogenesis	Human	Boutté et al. (2005)
Frontotemporal dementia and Parkinsonism associated with chromosome 17 and related tauopathies	A specific mutation affects microtubule in a site- and isoform-dependent manner	Indication of the reason for the diverse clinical pathologies of FTDP-17 and related tauopathies	COS cells	Sahara et al. (2000)
Down syndrome, Alzheimer’s disease and Pick's disease	Reduced number of individual protein components in the brain affecting cytoskeleton	Identification of cytoskeleton elements in normal brain and indication of cytoskeleton defects in patients	Human	Pollak et al. (2003)
Alzheimer’s disease and Pick's disease	Abnormal hyperphosphorylated tau aggregates influence β II-tubulin	High β II-tubulin content as a factor contributing to the disease development	Human	Puig et al. (2005)
Undefined tauopathy	Reduced stability of detyrosinated microtubules	Aggregation of tau protein affects microtubules	Primary cultures of rat astrocytes	Yoshiyama et al. (2003)
Undefined tauopathy	Fragmentation of the Golgi apparatus	The mechanical strength of tau-induced ring microtubule bundles	SH-SY5Y human neuroblastoma cells	Rodríguez-Cruz et al. (2018)
Undefined tauopathy	Microtubule loss	The cytotoxic potential of the protein associated with microtubule-binding repeats	Transgenic models of C. elegans	Miyasaka et al. (2018)
Undefined tauopathy	A chaperone E knockout system of tubulin	Involvement of disruption of tubulin biosynthesis in the accumulation of toxic tau protein	primary cultures of mouse neurons	Fujiwara et al. (2018)
Undefined tauopathy	Abnormal aggregation of tubulin under the influence of glyceraldehyde	Elucidation of the mechanism of glyceraldehyde action in neurodegeneration which may contribute to the development of new neuroprotective therapies	SH-SY5Y human neuroblastoma cells	Nasu et al. (2020)
Undefined tauopathy	Abnormal microtubule binding, change in the distribution of filamentous actin	Indication of a newly discovered mechanism of tau protein toxicity in tauopathies	C6 glial cells	Maasz et al. (2014)