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Book ChapterDOI

Regulation of microtubule-associated proteins

TLDR
This review summarizes the functional activities of MAPs found in animal cells and discusses how these MAPs are regulated.
Abstract
Microtubule-associated proteins (MAPs) function to regulate the assembly dynamics and organization of microtubule polymers. Upstream regulation of MAP activities is the major mechanism used by cells to modify and control microtubule assembly and organization. This review summarizes the functional activities of MAPs found in animal cells and discusses how these MAPs are regulated. Mechanisms controlling gene expression, isoform-specific expression, protein localization, phosphorylation, and degradation are discussed. Additional regulatory mechanisms include synergy or competition between MAPs and the activities of cofactors or binding partners. For each MAP it is likely that regulation in vivo reflects a composite of multiple regulatory mechanisms.

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Citations
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Journal ArticleDOI

Cytoskeletal dynamics and transport in growth cone motility and axon guidance

TL;DR: A working model for cytoskeletal regulation of directed axon outgrowth is presented and an important goal for the future will be to understand the coordinated response of the cytoskeleton to signaling cascades induced by guidance receptor activation.
Journal ArticleDOI

The MAP1 family of microtubule-associated proteins

TL;DR: Microtubule-associated proteins of the MAP2/Tau family include the vertebrate proteins MAP2, MAP4, and Tau and homologs in other animals and are best known for their microtubules-stabilizing activity and for proposed roles regulating microtubule networks in the axons and dendrites of neurons.
Journal ArticleDOI

Biochemistry and Cell Biology of Tau Protein in Neurofibrillary Degeneration

TL;DR: The pathological aggregation of Tau is counterintuitive, given its high solubility, but can be rationalized by short hydrophobic motifs forming β structures.
Journal ArticleDOI

Structural Polymorphism of 441-Residue Tau at Single Residue Resolution

TL;DR: The methodology reveals that 441-residue tau is highly dynamic in solution with a distinct domain character and an intricate network of transient long-range contacts important for pathogenic aggregation.
Journal ArticleDOI

Implications for Kinetochore-Microtubule Attachment from the Structure of an Engineered Ndc80 Complex

TL;DR: An engineered "bonsai" Ndc80 complex containing a shortened rod domain but retaining the globular domains required for kinetochore localization and microtubule binding is crystallized, revealing a microtubules-binding interface containing a pair of tightly interacting calponin-homology (CH) domains with a previously unknown arrangement.
References
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Journal ArticleDOI

Lessons from Hereditary Colorectal Cancer

TL;DR: The authors are grateful to the members of their laboratories for their contributions to the reviewed studies and to F. Giardiello and S. Hamilton for photographs of colorectal lesions.
Journal ArticleDOI

Dynamic instability of microtubule growth

TL;DR: It is reported here that microtubules in vitro coexist in growing and shrinking populations which interconvert rather infrequently and this dynamic instability is a general property of micro Tubules and may be fundamental in explaining cellular microtubule organization.
Journal ArticleDOI

A protein factor essential for microtubule assembly

TL;DR: The unique ability of tau to restore the normal features of in vitro microtubules assembly makes it likely that tau is a major regulator of microtubule formation in cells.
Journal ArticleDOI

Multiple isoforms of human microtubule-associated protein tau: sequences and localization in neurofibrillary tangles of Alzheimer's disease

TL;DR: Antisera raised against synthetic peptides corresponding to these different human tau isoforms demonstrate that multiple tau protein isoforms are incorporated into the neurofibrillary tangles of Alzheimer's disease.
Journal ArticleDOI

Structure of the alpha beta tubulin dimer by electron crystallography.

TL;DR: An atomic model of the αβ tubulin dimer fitted to a 3.7-Å density map obtained by electron crystallography of zinc-induced tubulin sheets is presented.
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