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J Cell Biol
1986 Jun 01;1026:2106-14. doi: 10.1083/jcb.102.6.2106.
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A cloned cDNA encoding MAP1 detects a single copy gene in mouse and a brain-abundant RNA whose level decreases during development.
Lewis SA
,
Sherline P
,
Cowan NJ
.
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Screening of a bacteriophage lambda gt11 cDNA expression library with a polyclonal anti-microtubule associated protein (MAP) antiserum resulted in the isolation of two non-cross-hybridizing sets of cDNA clones. One set was shown to encode MAP2 (Lewis, S. A., A. Villasante, P. Sherline, and N. J. Cowan, 1986, J. Cell Biol., 102:2098-2105). To determine the specificity of the second set, three non-overlapping fragments cloned from the same mRNA molecule via a series of "walking" experiments were separately subcloned into inducible plasmid expression vectors in the appropriate orientation and reading frame. Upon induction and analysis by immunoblotting, two of the fusion proteins synthesized were shown to be immunoreactive with an anti-MAP1-specific antibody, but not with an anti-MAP2-specific antibody. Since these MAP1-specific epitopes are encoded in non-overlapping cDNAs cloned from a single contiguous mRNA, these clones cannot encode polypeptides that contain adventitiously cross-reactive epitopes. Furthermore, these cDNA clones detected an abundant mRNA species of greater than 10 kb in mouse brain, consistent with the coding requirement of a 350,000-D polypeptide and the known abundance of MAP1 in that tissue. The MAP1-specific cDNA probes were used in blot transfer experiments with RNA prepared from brain, liver, kidney, stomach, spleen, and thymus. While detectable quantities of MAP1-specific mRNA were observed in these tissues, the level of MAP1 expression was approximately 500-fold lower than in brain. The levels of both MAP1-specific and MAP2-specific mRNAs decline in the postnatal developing brain; the level of MAP1-specific mRNA also increases slightly in rat PC12 cells upon exposure to nerve growth factor. These surprising results contrast sharply with reported dramatic developmental increases in the amount of MAP1 in brain and in nerve growth factor-induced PC12 cells. The cDNA clones encoding MAP1 detect a single copy sequence in mouse DNA, even under conditions of low stringency that would allow the detection of related but mismatched sequences. The cDNAs cross-hybridize with genomic sequences in rat, human, and chicken DNA, but not with DNA from frog, Drosophila, or sea urchin. These data are discussed in terms of the evolution and possible biological role of MAP1.
Amara,
Alternative RNA processing in calcitonin gene expression generates mRNAs encoding different polypeptide products.
1982, Pubmed
Amara,
Alternative RNA processing in calcitonin gene expression generates mRNAs encoding different polypeptide products.
1982,
Pubmed
Amos,
Arrangement of high molecular weight associated proteins on purified mammalian brain microtubules.
1977,
Pubmed
Asai,
Microtubule-associated proteins (MAPs): a monoclonal antibody to MAP 1 decorates microtubules in vitro but stains stress fibers and not microtubules in vivo.
1985,
Pubmed
Berk,
Spliced early mRNAs of simian virus 40.
1978,
Pubmed
Bernhardt,
Differences in the developmental patterns of three microtubule-associated proteins in the rat cerebellum.
1985,
Pubmed
Bloom,
Microtubule-associated protein 1B: identification of a major component of the neuronal cytoskeleton.
1985,
Pubmed
Bloom,
Widespread cellular distribution of MAP-1A (microtubule-associated protein 1A) in the mitotic spindle and on interphase microtubules.
1984,
Pubmed
Borisy,
Purification of tubulin and associated high molecular weight proteins from porcine brain and characterization of microtubule assembly in vitro.
1975,
Pubmed
Cleveland,
Number and evolutionary conservation of alpha- and beta-tubulin and cytoplasmic beta- and gamma-actin genes using specific cloned cDNA probes.
1980,
Pubmed
,
Echinobase
De Brabander,
Immunoelectron microscopic localization of the 210,000-mol wt microtubule-associated protein in cultured cells of primates.
1981,
Pubmed
Dentler,
Ultrastructural localization of the high molecular weight proteins associated with in vitro-assembled brain microtubules.
1975,
Pubmed
Drubin,
Nerve growth factor-induced neurite outgrowth in PC12 cells involves the coordinate induction of microtubule assembly and assembly-promoting factors.
1985,
Pubmed
Greene,
Regulation of a high molecular weight microtubule-associated protein in PC12 cells by nerve growth factor.
1983,
Pubmed
Herrmann,
Microheterogeneity of microtubule-associated proteins, MAP-1 and MAP-2, and differential phosphorylation of individual subcomponents.
1985,
Pubmed
Herzog,
Fractionation of brain microtubule-associated proteins. Isolation of two different proteins which stimulate tubulin polymerization in vitro.
1978,
Pubmed
Huber,
Differences in the cellular distributions of two microtubule-associated proteins, MAP1 and MAP2, in rat brain.
1984,
Pubmed
Huber,
Immunocytochemical localization of microtubule-associated protein 1 in rat cerebellum using monoclonal antibodies.
1984,
Pubmed
Kim,
Stable reduction of thymidine kinase activity in cells expressing high levels of anti-sense RNA.
1985,
Pubmed
Kim,
The periodic association of MAP2 with brain microtubules in vitro.
1979,
Pubmed
Lewis,
Brain-specific expression of MAP2 detected using a cloned cDNA probe.
1986,
Pubmed
,
Echinobase
Murphy,
Association of high-molecular-weight proteins with microtubules and their role in microtubule assembly in vitro.
1975,
Pubmed
Riederer,
Differential expression of distinct microtubule-associated proteins during brain development.
1985,
Pubmed
Rigby,
Labeling deoxyribonucleic acid to high specific activity in vitro by nick translation with DNA polymerase I.
1977,
Pubmed
Schwarzbauer,
Three different fibronectin mRNAs arise by alternative splicing within the coding region.
1983,
Pubmed
Sherline,
Immunofluorescence localization of proteins of high molecular weight along intracellular microtubules.
1977,
Pubmed
Sloboda,
Microtubule-associated proteins and the stimulation of tubulin assembly in vitro.
1976,
Pubmed
Southern,
Detection of specific sequences among DNA fragments separated by gel electrophoresis.
1975,
Pubmed
Vallee,
Removal of the projections from cytoplasmic microtubules in vitro by digestion with trypsin.
1977,
Pubmed
Voter,
Electron microscopy of MAP 2 (microtubule-associated protein 2).
1982,
Pubmed
Wiche,
Widespread occurrence of polypeptides related to neurotubule-associated proteins (MAP-1 and MAP-2) in non-neuronal cells and tissues.
1984,
Pubmed