High-<i>M</i>r microtubule-associated proteins: properties and functions

Wiche, Gerhard

doi:10.1042/bj2590001

Cited by 107 publications

(58 citation statements)

References 153 publications

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“…MAPs are associated with microtubules in vitro and in vivo and have been shown to alter microtubule assembly dynamics [3][4][5]10,25] and microtubule flexibility, although their effect on flexibility remains controversial [6,20,21]. These effects coupled with the spatial and temporal distribution of MAPs are generally considered to be important for the development and maintenance of cellular morphology.…”

Section: Discussionmentioning

confidence: 99%

“…Indeed, MAPs have been implicated in both increasing microtubule rigidity and altering microtubule dynamics [3,5,6] and several MAPs have been shown to be spatially and temporally regulated [4]. For example, high molecular weight MAP2 is found essentially in dendrites and transfection of MAP2 in non-neuronal cell lines causes bundling of microtubules and increased rigidity [7], an ability which may be important for promotion of process outgrowth.…”

Section: Introductionmentioning

confidence: 99%

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Modulation of microtubule shape in vitro by high molecular weight microtubule associated proteins MAP1A, MAP1B, and MAP2

et al. 1996

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The effect of microtubule associated proteins on microtubule shape has been investigated in reconstitution experiments using purified tubulin and purified MAP1A, MAP1B, and MAP2. Microtubules assembled in the presence of these MAPs were fixed with 0.1% glutaraldehyde and, after negative staining, were examined by electron microscopy. The results show that MAP1A microtubules were generally short and 'straight' while those assembled with MAP1B were longer and 'bendy'. MAP2 microtubnies showed both types of morphologies even though straight microtubules were more abundant. These data suggest that MAPs may modulate not only microtubnie dynamics but also microtubule shape which may be important in their spatial distribution and/or role in specific neuronal areas.

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Section: Discussionmentioning

confidence: 99%

Section: Introductionmentioning

confidence: 99%

Modulation of microtubule shape in vitro by high molecular weight microtubule associated proteins MAP1A, MAP1B, and MAP2

et al. 1996

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“…MAP2, in that it is mainly present in neurons at early developmental stages and in the relative inefficiency with which it co-sediments with microtubules in vitro. However, antisera against MAP1B immunostain microtubule networks in neuronal cells, axons and dendrites, and nonneuronal cell lines [1]. Immunoaffinity purified MAP1B has also been shown to bind to microtubules and to form long filamentous projections from the microtubule surface [3].…”

Section: Introductionmentioning

confidence: 99%

“…A heterogenous group of proteins (MAPs) normally associated with microtubules have been suggested to play an important role in the growth and maintenance of neuronal processes [1]. Microtubule associated protein 1B (MAP1B, also known as MAP1X, MAP1.2, MAP5; [2])differs from most high molecular weight MAPs, e.g.…”

Section: Introductionmentioning

confidence: 99%

Microtubule associated protein 1B (MAP1B) promotes efficient tubulin polymerisation in vitro

Pedrotti¹,

Islam²

1995

FEBS Letters

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The effect of MAP1B on tubulin polymerisation has been examined in reconstitution experiments using purified tubulin and MAP1B. Under the assembly conditions used, tubulin alone was incapable of polymerising, but addition of MAP1B resulted in rapid assembly into microtubules. The kinetics of MAP1B‐promoted microtubule assembly examined using pseudo‐first‐order plots show that assembly is described by a single reaction rate. The calculated association rate constant for MAP1B was about 200 × 106M−1·s−1 and this constant was one order of magnitude higher when compared with that for MAP2‐promoted assembly.

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“…The relation between monomers and polymers (normally 1:1) can be shifted very quickly. Secondly, actin filaments and microtubuli associate specific proteins (actin associated proteins: (6,7,9,24); microtubuli associated proteins: (4,(11)(12)(13). A large number of these proteins modify the structure and properties of the filaments and link them with other structures and with the plasma membrane (tab.…”

Section: Proteins Of the Cytoskeletonmentioning

confidence: 99%