Diverse Distribution and Function of Fibrous Microtubule-Associated Proteins in the Nervous System

Schoenfeld, Thomas A.; Obar, Robert A.

doi:10.1016/s0074-7696(08)62631-5

Cited by 110 publications

(74 citation statements)

References 267 publications

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“…: 43-1-4277-52858; Fax: 43-1-4277-52854; E-mail: friedrich.propst@univie.ac.at. 1 The abbreviations used are: MAP, microtubule-associated protein; GST, glutathione S-transferase; HC, heavy chain; LC, light chain; MH, MAP1 homology; PBS, phosphate-buffered saline; aa, amino acid(s); Pipes, 1,4-piperazinediethanesulfonic acid; BSA, bovine serum albumin.…”

Section: Cdna Constructsmentioning

confidence: 99%

“…The classical microtubule-associated proteins (MAPs) 1 MAP1, MAP2, and tau were discovered more than 20 years ago by virtue of the fact that they copurified with microtubules from vertebrate brain (1). Because of the developmental regulation of expression of these proteins, their restricted localization in the axonal or somato-dendritic compartment of neurons, and the differential phosphorylation depending on the developmental stage and subcellular localization, it was soon proposed that MAPs are important regulators of neuronal microtubules during differentiation.…”

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confidence: 99%

“…Both proteins are of high molecular mass (ϳ300 kDa, 2500 aa), are expressed predominantly in the nervous system, and consist of several subunits, one heavy chain (HC) and at least one light chain (LC) (1). In each case, heavy and light chains are the products of proteolytic cleavage of a common polyprotein precursor.…”

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confidence: 99%

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Microtubule-associated Protein 1S, a Short and Ubiquitously Expressed Member of the Microtubule-associated Protein 1 Family

Orbán-Németh

Simader

Badurek

et al. 2005

Journal of Biological Chemistry

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The related high molecular mass microtubuleassociated proteins (MAPs) MAP1A and MAP1B are predominantly expressed in the nervous system and are involved in axon guidance and synaptic function. MAP1B is implicated in fragile X mental retardation, giant axonal neuropathy, and ataxia type 1. We report the functional characterization of a novel member of the microtubule-associated protein 1 family, which we termed MAP1S (corresponding to sequence data bank entries for VCY2IP1 and C19ORF5). MAP1S contains the three hallmark domains of the microtubuleassociated protein 1 family but hardly any additional sequences. It decorates neuronal microtubules and copurifies with tubulin from brain. MAP1S is synthesized as a precursor protein that is partially cleaved into heavy and light chains in a tissue-specific manner. Heavy and light chains interact to form the MAP1S complex. The light chain binds, bundles, and stabilizes microtubules and binds to actin. The heavy chain appears to regulate light chain activity. In contrast to MAP1A and MAP1B, MAP1S is expressed in a wide range of tissues in addition to neurons and represents the non-neuronal counterpart of this cytolinker family.The classical microtubule-associated proteins (MAPs) 1 MAP1, MAP2, and tau were discovered more than 20 years ago by virtue of the fact that they copurified with microtubules from vertebrate brain (1). Because of the developmental regulation of expression of these proteins, their restricted localization in the axonal or somato-dendritic compartment of neurons, and the differential phosphorylation depending on the developmental stage and subcellular localization, it was soon proposed that MAPs are important regulators of neuronal microtubules during differentiation.The MAP1 family has two members: MAP1A and MAP1B. Both proteins are of high molecular mass (ϳ300 kDa, 2500 aa), are expressed predominantly in the nervous system, and consist of several subunits, one heavy chain (HC) and at least one light chain (LC) (1). In each case, heavy and light chains are the products of proteolytic cleavage of a common polyprotein precursor. MAP1A and MAP1B share three substantial regions of sequence homology (2), one in the NH 2 terminus of the heavy chains, one in the COOH terminus of the heavy chains, and one in the COOH-terminal half of the light chains. We termed these homologous hallmark domains of the MAP1 family MH1, MH2, and MH3, respectively. In MAP1B, the MH1 and MH3 domains mediate the interaction between heavy and light chains (3), and the MH3 domain of both proteins contains an actin binding site (4). MAP1A and MAP1B are conserved in vertebrates. A MAP1 ortholog termed Futsch has been identified in Drosophila (5).MAP1B function has been investigated by gene targeting in the mouse, and the original contention that it is important for neuronal differentiation and development of the nervous system has been confirmed (6 -9). Mice homozygous for hypomorphic or null alleles of MAP1B display defects in axonal guidance, neuronal migration, axon diameter, and ...

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Section: Cdna Constructsmentioning

confidence: 99%

mentioning

confidence: 99%

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Microtubule-associated Protein 1S, a Short and Ubiquitously Expressed Member of the Microtubule-associated Protein 1 Family

Orbán-Németh

Simader

Badurek

et al. 2005

Journal of Biological Chemistry

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“…Microtubule stability is thought to be modulated by a variety of post-translational modifications of both tubulin and MAPs. 1 Structural MAPs are filamentous proteins which bind to microtubules in a nucleotide-insensitive way, forming elongated projections from the microtubule surface (for reviews, see Olmsted (1991), Hirokawa (1994), Schoenfeld and Obar (1994), and Mandelkow and Mandelkow (1995)). MAPs can control microtubule dynamics in vitro and in vivo (Drechsel et al, 1992;Pryer et al, 1992;Umeyama et al, 1993;Gustke et al, 1994;Brandt et al, 1994;Dhamodharan and Wadsworth, 1995;Trinczek et al, 1995).…”

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confidence: 99%

Phosphorylation of Microtubule-associated Proteins MAP2 and MAP4 by the Protein Kinase p110mark

Illenberger

Drewes

Trinczek

et al. 1996

Journal of Biological Chemistry

185

173

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“…Classical MAPs, also called structural MAPs, were isolated more than 20 years ago from mammalian brains by copurification with MTs (Schoenfeld and Obar 1994). A general overview of domain structure of classical MAPs is given in Fig.…”

Section: Classical Mapsmentioning

confidence: 99%

Microtubule Organization and Microtubule-Associated Proteins (MAPs)

2016

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Dendrites have a unique microtubule organization. In vertebrates, dendritic microtubules are organized in antiparallel bundles, oriented with their plus ends either pointing away or toward the soma. The mixed microtubule arrays control intracellular trafficking and local signaling pathways, and are essential for dendrite development and function. The organization of microtubule arrays largely depends on the combined function of different microtubule regulatory factors or generally named microtubule-associated proteins (MAPs). Classical MAPs, also called structural MAPs, were identified more than 20 years ago based on their ability to bind to and copurify with microtubules. Most classical MAPs bind along the microtubule lattice and regulate microtubule polymerization, bundling, and stabilization. Recent evidences suggest that classical MAPs also guide motor protein transport, interact with the actin cytoskeleton, and act in various neuronal signaling networks. Here, we give an overview of microtubule organization in dendrites and the role of classical MAPs in dendrite development, dendritic spine formation, and synaptic plasticity. IntroductionMicrotubules (MTs) are cytoskeletal structures that play essential roles in all eukaryotic cells. MTs are important not only during cell division but also in non-dividing cells, where they are critical structures in numerous cellular processes such as cell motility, migration, differentiation, intracellular transport and organelle positioning. MTs are composed of two proteins, α-and β-tubulin, that form heterodimers and organize themselves in a head-to-tail manner. MTs are dynamic and they can rapidly switch between cycles of growth and shrinkage. This MT

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Diverse Distribution and Function of Fibrous Microtubule-Associated Proteins in the Nervous System

Cited by 110 publications

References 267 publications

Microtubule-associated Protein 1S, a Short and Ubiquitously Expressed Member of the Microtubule-associated Protein 1 Family

Microtubule-associated Protein 1S, a Short and Ubiquitously Expressed Member of the Microtubule-associated Protein 1 Family

Phosphorylation of Microtubule-associated Proteins MAP2 and MAP4 by the Protein Kinase p110mark

Microtubule Organization and Microtubule-Associated Proteins (MAPs)

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