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  1. Article: Trafficking of signaling modules by kinesin motors.

    Schnapp, Bruce J

    Journal of cell science

    2003  Volume 116, Issue Pt 11, Page(s) 2125–2135

    Abstract: The human genome has more than 40 kinesin genes whose protein products organize intracellular traffic along microtubules. Research during the past two years has begun to elucidate the cargoes carried by kinesins and the nature of the kinesin-cargo ... ...

    Abstract The human genome has more than 40 kinesin genes whose protein products organize intracellular traffic along microtubules. Research during the past two years has begun to elucidate the cargoes carried by kinesins and the nature of the kinesin-cargo linkage. Modular protein-protein interactions connect kinesins to diverse cellular molecules, which, apart from their other functions, serve as kinesin-cargo linkers. Many of these newly identified linkers are scaffolds for signaling pathways, and mounting evidence now indicates that kinesins transport pre-assembled signaling modules as vesicular cargo. These findings bring together two fields, signal transduction and molecular motors, and lead to a deeper understanding of the interplay between trafficking, localization and intercellular communication.
    MeSH term(s) Animals ; Humans ; Kinesin/physiology ; Molecular Motor Proteins/physiology ; Protein Transport/physiology ; Signal Transduction/physiology
    Chemical Substances Molecular Motor Proteins ; Kinesin (EC 3.6.4.4)
    Language English
    Publishing date 2003-06-01
    Publishing country England
    Document type Journal Article ; Research Support, Non-U.S. Gov't ; Research Support, U.S. Gov't, Non-P.H.S. ; Research Support, U.S. Gov't, P.H.S. ; Review
    ZDB-ID 2993-2
    ISSN 1477-9137 ; 0021-9533
    ISSN (online) 1477-9137
    ISSN 0021-9533
    DOI 10.1242/jcs.00488
    Database MEDical Literature Analysis and Retrieval System OnLINE

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  2. Article: A repeated IMP-binding motif controls oskar mRNA translation and anchoring independently of Drosophila melanogaster IMP.

    Munro, Trent P / Kwon, Sunjong / Schnapp, Bruce J / St Johnston, Daniel

    The Journal of cell biology

    2006  Volume 172, Issue 4, Page(s) 577–588

    Abstract: Zip code-binding protein 1 (ZBP-1) and its Xenopus laevis homologue, Vg1 RNA and endoplasmic reticulum-associated protein (VERA)/Vg1 RNA-binding protein (RBP), bind repeated motifs in the 3' untranslated regions (UTRs) of localized mRNAs. Although these ... ...

    Abstract Zip code-binding protein 1 (ZBP-1) and its Xenopus laevis homologue, Vg1 RNA and endoplasmic reticulum-associated protein (VERA)/Vg1 RNA-binding protein (RBP), bind repeated motifs in the 3' untranslated regions (UTRs) of localized mRNAs. Although these motifs are required for RNA localization, the necessity of ZBP-1/VERA remains unresolved. We address the role of ZBP-1/VERA through analysis of the Drosophila melanogaster homologue insulin growth factor II mRNA-binding protein (IMP). Using systematic evolution of ligands by exponential enrichment, we identified the IMP-binding element (IBE) UUUAY, a motif that occurs 13 times in the oskar 3'UTR. IMP colocalizes with oskar mRNA at the oocyte posterior, and this depends on the IBEs. Furthermore, mutation of all, or subsets of, the IBEs prevents oskar mRNA translation and anchoring at the posterior. However, oocytes lacking IMP localize and translate oskar mRNA normally, illustrating that one cannot necessarily infer the function of an RBP from mutations in its binding sites. Thus, the translational activation of oskar mRNA must depend on the binding of another factor to the IBEs, and IMP may serve a different purpose, such as masking IBEs in RNAs where they occur by chance. Our findings establish a parallel requirement for IBEs in the regulation of localized maternal mRNAs in D. melanogaster and X. laevis.
    MeSH term(s) 3' Untranslated Regions/metabolism ; Amino Acid Motifs ; Animals ; Base Sequence ; Binding Sites ; Drosophila Proteins/analysis ; Drosophila Proteins/genetics ; Drosophila Proteins/metabolism ; Drosophila melanogaster ; Molecular Sequence Data ; Mutation ; Oocytes/chemistry ; Protein Biosynthesis ; RNA, Messenger/biosynthesis ; RNA-Binding Proteins/analysis ; RNA-Binding Proteins/genetics ; RNA-Binding Proteins/metabolism
    Chemical Substances 3' Untranslated Regions ; Drosophila Proteins ; Imp protein, Drosophila ; RNA, Messenger ; RNA-Binding Proteins ; osk protein, Drosophila
    Language English
    Publishing date 2006-02-08
    Publishing country United States
    Document type Journal Article ; Research Support, N.I.H., Extramural ; Research Support, Non-U.S. Gov't
    ZDB-ID 218154-x
    ISSN 1540-8140 ; 0021-9525
    ISSN (online) 1540-8140
    ISSN 0021-9525
    DOI 10.1083/jcb.200510044
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  3. Article: Zebrafish melanophilin facilitates melanosome dispersion by regulating dynein.

    Sheets, Lavinia / Ransom, David G / Mellgren, Eve M / Johnson, Stephen L / Schnapp, Bruce J

    Current biology : CB

    2007  Volume 17, Issue 20, Page(s) 1721–1734

    Abstract: Background: Fish melanocytes aggregate or disperse their melanosomes in response to the level of intracellular cAMP. The role of cAMP is to regulate both melanosome travel along microtubules and their transfer between microtubules and actin. The factors ...

    Abstract Background: Fish melanocytes aggregate or disperse their melanosomes in response to the level of intracellular cAMP. The role of cAMP is to regulate both melanosome travel along microtubules and their transfer between microtubules and actin. The factors that are downstream of cAMP and that directly modulate the motors responsible for melanosome transport are not known. To identify these factors, we are characterizing melanosome transport mutants in zebrafish.
    Results: We report that a mutation (allele j120) in the gene encoding zebrafish melanophilin (Mlpha) interferes with melanosome dispersion downstream of cAMP. Based on mouse genetics, the current model of melanophilin function is that melanophilin links myosin V to melanosomes. The residues responsible for this function are conserved in the zebrafish ortholog. However, if linking myosin V to melanosomes was Mlpha's sole function, elevated cAMP would cause mlpha(j120) mutant melanocytes to hyperdisperse their melanosomes. Yet this is not what we observe. Instead, mutant melanocytes disperse their melanosomes much more slowly than normal and less than halfway to the cell margin. This defect is caused by a failure to suppress minus-end (dynein) motility along microtubules, as shown by tracking individual melanosomes. Disrupting the actin cytoskeleton, which causes wild-type melanocytes to hyperdisperse their melanosomes, does not affect dispersion in mutant melanocytes. Therefore, Mlpha regulates dynein independently of its putative linkage to myosin V.
    Conclusions: We propose that cAMP-induced melanosome dispersion depends on the actin-independent suppression of dynein by Mlpha and that Mlpha coordinates the early outward movement of melanosomes along microtubules and their later transfer to actin filaments.
    MeSH term(s) Amino Acid Sequence ; Animals ; Base Sequence ; Biological Transport, Active/drug effects ; Carrier Proteins/genetics ; Carrier Proteins/physiology ; DNA Primers/genetics ; Dyneins/physiology ; Hypothalamic Hormones/pharmacology ; Melanins/pharmacology ; Melanocyte-Stimulating Hormones/pharmacology ; Melanocytes/drug effects ; Melanocytes/physiology ; Melanocytes/ultrastructure ; Melanosomes/drug effects ; Melanosomes/physiology ; Microtubules/drug effects ; Microtubules/physiology ; Models, Biological ; Molecular Sequence Data ; Mutation ; Phylogeny ; Pigmentation/drug effects ; Pigmentation/genetics ; Pigmentation/physiology ; Pituitary Hormones/pharmacology ; Sequence Homology, Amino Acid ; Zebrafish/genetics ; Zebrafish/physiology ; Zebrafish Proteins/genetics ; Zebrafish Proteins/physiology
    Chemical Substances Carrier Proteins ; DNA Primers ; Hypothalamic Hormones ; Melanins ; Pituitary Hormones ; Zebrafish Proteins ; melanin-concentrating hormone (67382-96-1) ; Melanocyte-Stimulating Hormones (9002-79-3) ; Dyneins (EC 3.6.4.2)
    Language English
    Publishing date 2007-10-04
    Publishing country England
    Document type Journal Article ; Research Support, N.I.H., Extramural
    ZDB-ID 1071731-6
    ISSN 1879-0445 ; 0960-9822
    ISSN (online) 1879-0445
    ISSN 0960-9822
    DOI 10.1016/j.cub.2007.09.028
    Database MEDical Literature Analysis and Retrieval System OnLINE

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  4. Article ; Online: Optimized Filter Set and Viewing Conditions for the S65T Mutant of GFP in Living Cells

    Mark J. Zylka / Bruce J. Schnapp

    BioTechniques, Vol 21, Iss 2, Pp 220-

    1996  Volume 226

    Keywords Biology (General) ; QH301-705.5
    Language English
    Publishing date 1996-08-01T00:00:00Z
    Publisher Future Science Ltd
    Document type Article ; Online
    Database BASE - Bielefeld Academic Search Engine (life sciences selection)

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  5. Article: UUCAC- and vera-dependent localization of VegT RNA in Xenopus oocytes.

    Kwon, Sunjong / Abramson, Tatiana / Munro, Trent P / John, Corinne M / Köhrmann, Martin / Schnapp, Bruce J

    Current biology : CB

    2002  Volume 12, Issue 7, Page(s) 558–564

    Abstract: Localized mRNAs are directed to their destinations by "localization elements" (LEs) in their 3'UTRs. LEs harbor multiple, functionally redundant localization "signals." These signals are poorly defined, hence it is unclear whether the signals-and their ... ...

    Abstract Localized mRNAs are directed to their destinations by "localization elements" (LEs) in their 3'UTRs. LEs harbor multiple, functionally redundant localization "signals." These signals are poorly defined, hence it is unclear whether the signals-and their cognate factors-are unique to each RNA or employed generally. Five "E2s" (UUCACs) in the 366 nt Vg1 LE (VgLE) direct this transcript to the vegetal pole of Xenopus oocytes via the binding of a protein-Vera/Vg1RBP/ZBP. Here we show that a different vegetal RNA, VegT, employs the same signal and factor. Five E2s within a 440 nt subregion (VegT440) of the VegT 3'UTR predict its LE and are both necessary and sufficient (in the context of antisense VegT440) for directing localization. The E2s in VegT440 and VgLE function similarly to recruit Vera protein: (1) in both contexts, E2 nt substitutions partially (UU to AC) or completely (CA to UG) inhibit localization in accordance with the sequence selectivity of Vera protein for E2s; (2) VegT440 and VgLE crosscompete, in an E2-dependent manner, for localization and Vera binding; (3) injection of anti-Vera antibody into oocytes inhibits localization of both injected transcripts. These findings imply that general localization signals traffic diverse RNAs.
    MeSH term(s) 3' Untranslated Regions/physiology ; Animals ; Base Sequence ; Biological Transport ; Glycoproteins/genetics ; Molecular Sequence Data ; Repetitive Sequences, Nucleic Acid/physiology ; T-Box Domain Proteins/genetics ; Transforming Growth Factor beta ; Xenopus Proteins ; Xenopus laevis
    Chemical Substances 3' Untranslated Regions ; GDF1 protein, Xenopus ; Glycoproteins ; T-Box Domain Proteins ; Transforming Growth Factor beta ; VegT protein, Xenopus ; Xenopus Proteins
    Language English
    Publishing date 2002-04-02
    Publishing country England
    Document type Journal Article ; Research Support, U.S. Gov't, P.H.S.
    ZDB-ID 1071731-6
    ISSN 1879-0445 ; 0960-9822
    ISSN (online) 1879-0445
    ISSN 0960-9822
    DOI 10.1016/s0960-9822(02)00740-6
    Database MEDical Literature Analysis and Retrieval System OnLINE

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  6. Article: A repeated IMP-binding motif controls oskar mRNA translation and anchoring independently of Drosophila melanogaster IMP

    Munro, Trent P / Kwon, Sunjong / Schnapp, Bruce J / St Johnston, Daniel

    Journal of cell biology. 2006 Feb. 13, v. 172, no. 4

    2006  

    Abstract: Zip code-binding protein 1 (ZBP-1) and its Xenopus laevis homologue, Vg1 RNA and endoplasmic reticulum-associated protein (VERA)/Vg1 RNA-binding protein (RBP), bind repeated motifs in the 3' untranslated regions (UTRs) of localized mRNAs. Although these ... ...

    Abstract Zip code-binding protein 1 (ZBP-1) and its Xenopus laevis homologue, Vg1 RNA and endoplasmic reticulum-associated protein (VERA)/Vg1 RNA-binding protein (RBP), bind repeated motifs in the 3' untranslated regions (UTRs) of localized mRNAs. Although these motifs are required for RNA localization, the necessity of ZBP-1/VERA remains unresolved. We address the role of ZBP-1/VERA through analysis of the Drosophila melanogaster homologue insulin growth factor II mRNA-binding protein (IMP). Using systematic evolution of ligands by exponential enrichment, we identified the IMP-binding element (IBE) UUUAY, a motif that occurs 13 times in the oskar 3'UTR. IMP colocalizes with oskar mRNA at the oocyte posterior, and this depends on the IBEs. Furthermore, mutation of all, or subsets of, the IBEs prevents oskar mRNA translation and anchoring at the posterior. However, oocytes lacking IMP localize and translate oskar mRNA normally, illustrating that one cannot necessarily infer the function of an RBP from mutations in its binding sites. Thus, the translational activation of oskar mRNA must depend on the binding of another factor to the IBEs, and IMP may serve a different purpose, such as masking IBEs in RNAs where they occur by chance. Our findings establish a parallel requirement for IBEs in the regulation of localized maternal mRNAs in D. melanogaster and X. laevis.
    Language English
    Dates of publication 2006-0213
    Size p. 577-588.
    Document type Article
    ZDB-ID 218154-x
    ISSN 1540-8140 ; 0021-9525
    ISSN (online) 1540-8140
    ISSN 0021-9525
    Database NAL-Catalogue (AGRICOLA)

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