Recombinant Mouse Microtubule-associated protein tau (Mapt) (Active)

Function

Promotes microtubule assembly and stability, and might be involved in the establishment and maintenance of neuronal polarity. The C-terminus binds axonal microtubules while the N-terminus binds neural plasma membrane components, suggesting that tau functions as a linker protein between both. Axonal polarity is predetermined by tau localization (in the neuronal cell) in the domain of the cell body defined by the centrosome. The short isoforms allow plasticity of the cytoskeleton whereas the longer isoforms may preferentially play a role in its stabilization

Subcellular Location

Cytoplasm, cytosol; Cell membrane (Peripheral membrane protein); Cytoplasm, cytoskeleton; Cell projection, axon; Cell projection, dendrite; Secreted

Disease Association

[May be involved in the pathogenesis of cytoplasmic inclusions (as Mallory bodies) in livers of mice chronically intoxicated with Griseofulvin or DDC (3,5-diethoxycarbonyl-2,4-dihydrocollidine), a model for human alcoholic hepatitis. Alteration of Tau (abnormal phosphorylation and cross-linking) could contribute to Mallory bodies formation and disturbance of microtubule function in alcoholic liver disease]

Tissue Specificity

Expressed in neurons and at a lower level in the liver and kidney. Isoform PNS-tau is expressed in the peripheral nervous system while the others are expressed in the central nervous system

Subunit

Interacts with MARK1, MARK2, MARK3 and MARK4 (By similarity). Interacts with SQSTM1 when polyubiquitinated (PubMed:15953362). Interacts with PSMC2 through SQSTM1 (PubMed:15953362). Interacts with FKBP4 (By similarity). Binds to CSNK1D (By similarity). Interacts with SGK1 (By similarity). Interacts with EPM2A; the interaction dephosphorylates MAPT at Ser-369 (By similarity). Interacts with PIN1 (By similarity). Interacts with LRRK2 (By similarity). Interacts with LRP1, leading to endocytosis; this interaction is reduced in the presence of LRPAP1/RAP (By similarity)

• Couchie D. et al. Primary structure of high molecular weight tau present in the peripheral nervous system. — Proc. Natl. Acad. Sci. U.S.A. (1992)
• Kenner L. et al. Expression of three- and four-repeat tau isoforms in mouse liver. — Hepatology (1994)
• Lee G. et al. The primary structure and heterogeneity of tau protein from mouse brain. — Science (1988)
• Sawa A. et al. Molecular diversity at the carboxyl terminus of human and rat tau. — Brain Res. Mol. Brain Res. (1994)
• Church D.M. et al. Lineage-specific biology revealed by a finished genome assembly of the mouse. — PLoS Biol. (2009)
• The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC). — Genome Res. (2004)
• Lubec G. et al. PubMed: CI-DHLEILD3HP6AK (JAN-)
• Couchie D. et al. High molecular weight tau proteins and acquisition of neuronal polarity in peripheral nervous system. — C. R. Acad. Sci. III, Sci. Vie (1993)