MAP 2 ( microtubule - associated protein 2 )
نویسندگان
چکیده
Four transcription variants have been characterized. MAP2 Isoform 5 (NM_001039538.1 --> NP_001034627.1): The difference in this isoform is characterized by the 5' UTR which results in the production of a longer protein when compared to isoform 2. MAP2 Isoform 1 (NM_002374.3 --> NP_002365.3): This isoform is thought to be the longest encoded and contains three alternative in-frame exons when compared to isoform 2. The tubulin binding and MAP2 projection domains are conserved. MAP2 Isoform 2 (NM_031845.2 --> NP_114033.2): This is the shortest transcript. MAP2 Isoform 4 (NM_031847.2 --> NP_114035.2): One alternate in-frame exon compared to isoform 2.
منابع مشابه
Analysis of the microtubule-binding domain of MAP-2
We examined the microtubule-binding domain of the microtubule-associated protein (MAP), MAP-2, using rabbit antibodies that specifically bind to the microtubule-binding region ("stub") and the projection portion ("arm") of MAP-2. We found that (a) microtubules decorated with arm antibody look similar to those labeled with whole unfractionated MAP antibody, though microtubules are not labeled wi...
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Objective(s):EMAP-like Protein 5 (EML5) is a new echinoderm microtubule-associated protein that is expressed in the central nervous system. The aim of this study was to investigate the expression profile of EML5 in the anterior temporal neocortex of patients presenting with intractable epilepsy (IE). Materials and Methods:Western blot assays were performed to determine EML5 expression in 36 su...
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In previous work we have demonstrated that the microtubule-associated protein 2 (MAP 2) molecule consists of two structural parts. One part of the molecule, referred to as the assembly-promoting domain, binds to the microtubule surface and is responsible for promoting microtubule assembly; the other represents a filamentous projection observed on the microtubule surface that may be involved in ...
متن کاملPhosphorylation of microtubule-associated proteins regulates their interaction with actin filaments.
We have determined the absolute phosphate content of microtubule-associated proteins (MAPs) and established that phosphorylation inhibits the actin filament cross-linking activity of MAPs and both of the major MAP components, MAP-2 and tau. Similar results were obtained with actin from rabbit muscle, hog brain, and Acanthamoeba castellanii. We used the endogenous phosphatases and kinases in hog...
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Thrombin cleavage of bovine brain microtubule-associated protein (MAP-2) yields two stable limit polypeptide fragments (28,000 and 240,000 Mr). The smaller cleavage product contains the microtubule-binding domain and is derived from the carboxyl terminus of MAP-2 while the 240,000 Mr fragment is derived from the amino terminus. The amino terminal sequence of the smaller cleavage product is homo...
متن کاملExtensive cAMP-dependent and cAMP-independent phosphorylation of microtubule-associated protein 2.
Microtubule-associated protein 2 (MAP 2) is the major substrate for phosphorylation in purified preparations of brain microtubules. In earlier work, we showed that phosphorylation is catalyzed by a type II cAMP-dependent protein kinase tightly associated with MAP 2 itself. In the present study, we have examined the extent of MAP 2 phosphorylation by its associated protein kinase. Using an inorg...
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