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  1. Article ; Online: Angiomotin isoform 2 promotes binding of PALS1 to KIF13B at primary cilia and regulates ciliary length and signaling.

    Morthorst, Stine Kjær / Nielsen, Camilla / Farinelli, Pietro / Anvarian, Zeinab / Rasmussen, Christina Birgitte R / Serra-Marques, Andrea / Grigoriev, Ilya / Altelaar, Maarten / Fürstenberg, Nicoline / Ludwig, Alexander / Akhmanova, Anna / Christensen, Søren Tvorup / Pedersen, Lotte Bang

    Journal of cell science

    2022  Volume 135, Issue 12

    Abstract: The kinesin-3 motor KIF13B functions in endocytosis, vesicle transport and regulation of ciliary length and signaling. Direct binding of the membrane-associated guanylate kinase (MAGUK) DLG1 to the MAGUK-binding stalk domain of KIF13B relieves motor ... ...

    Abstract The kinesin-3 motor KIF13B functions in endocytosis, vesicle transport and regulation of ciliary length and signaling. Direct binding of the membrane-associated guanylate kinase (MAGUK) DLG1 to the MAGUK-binding stalk domain of KIF13B relieves motor autoinhibition and promotes microtubule plus-end-directed cargo transport. Here, we characterize angiomotin (AMOT) isoform 2 (p80, referred to as Ap80) as a novel KIF13B interactor that promotes binding of another MAGUK, the polarity protein and Crumbs complex component PALS1, to KIF13B. Live-cell imaging analysis indicated that Ap80 is concentrated at and recruits PALS1 to the base of the primary cilium, but is not a cargo of KIF13B itself. Consistent with a ciliary function for Ap80, its depletion led to elongated primary cilia and reduced agonist-induced ciliary accumulation of SMO, a key component of the Hedgehog signaling pathway, whereas Ap80 overexpression caused ciliary shortening. Our results suggest that Ap80 activates KIF13B cargo binding at the base of the primary cilium to regulate ciliary length, composition and signaling.
    MeSH term(s) Angiomotins ; Cilia/metabolism ; Guanylate Kinases ; Hedgehog Proteins/metabolism ; Membrane Proteins/metabolism ; Protein Isoforms
    Chemical Substances Angiomotins ; Hedgehog Proteins ; Membrane Proteins ; Protein Isoforms ; Guanylate Kinases (EC 2.7.4.8)
    Language English
    Publishing date 2022-06-24
    Publishing country England
    Document type Journal Article ; Research Support, Non-U.S. Gov't
    ZDB-ID 2993-2
    ISSN 1477-9137 ; 0021-9533
    ISSN (online) 1477-9137
    ISSN 0021-9533
    DOI 10.1242/jcs.259471
    Database MEDical Literature Analysis and Retrieval System OnLINE

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  2. Article ; Online: KIF13B establishes a CAV1-enriched microdomain at the ciliary transition zone to promote Sonic hedgehog signalling.

    Schou, Kenneth B / Mogensen, Johanne B / Morthorst, Stine K / Nielsen, Brian S / Aleliunaite, Aiste / Serra-Marques, Andrea / Fürstenberg, Nicoline / Saunier, Sophie / Bizet, Albane A / Veland, Iben R / Akhmanova, Anna / Christensen, Søren T / Pedersen, Lotte B

    Nature communications

    2017  Volume 8, Page(s) 14177

    Abstract: Ciliary membrane composition is controlled by transition zone (TZ) proteins such as RPGRIP1, RPGRIPL and NPHP4, which are vital for balanced coordination of diverse signalling systems like the Sonic hedgehog (Shh) pathway. Activation of this pathway ... ...

    Abstract Ciliary membrane composition is controlled by transition zone (TZ) proteins such as RPGRIP1, RPGRIPL and NPHP4, which are vital for balanced coordination of diverse signalling systems like the Sonic hedgehog (Shh) pathway. Activation of this pathway involves Shh-induced ciliary accumulation of Smoothened (SMO), which is disrupted by disease-causing mutations in TZ components. Here we identify kinesin-3 motor protein KIF13B as a novel member of the RPGRIP1N-C2 domain-containing protein family and show that KIF13B regulates TZ membrane composition and ciliary SMO accumulation. KIF13B is upregulated during ciliogenesis and is recruited to the ciliary base by NPHP4, which binds to two distinct sites in the KIF13B tail region, including an RPGRIP1N-C2 domain. KIF13B and NPHP4 are both essential for establishment of a CAV1 membrane microdomain at the TZ, which in turn is required for Shh-induced ciliary SMO accumulation. Thus KIF13B is a novel regulator of ciliary TZ configuration, membrane composition and Shh signalling.
    MeSH term(s) Animals ; Caveolin 1/metabolism ; Cell Line ; Cell Membrane/metabolism ; Cell Membrane/physiology ; Cilia/physiology ; Computational Biology ; Gene Expression Profiling ; Gene Expression Regulation/physiology ; Gene Knockout Techniques ; HEK293 Cells ; Hedgehog Proteins/metabolism ; Humans ; Kinesin/genetics ; Kinesin/metabolism ; Membrane Proteins/genetics ; Membrane Proteins/metabolism ; Mice ; NIH 3T3 Cells ; Protein Domains/physiology ; Proteins/metabolism ; Signal Transduction/physiology ; Smoothened Receptor/metabolism ; Up-Regulation ; Zinc Finger Protein GLI1/genetics ; Zinc Finger Protein GLI1/metabolism
    Chemical Substances CAV1 protein, human ; Caveolin 1 ; GLI1 protein, human ; Hedgehog Proteins ; Membrane Proteins ; NPHP4 protein, human ; NPHP4 protein, mouse ; Proteins ; SHH protein, human ; SMO protein, human ; Smoothened Receptor ; Zinc Finger Protein GLI1 ; KIF13B protein, human (EC 3.6.1.-) ; KIF13b protein, mouse (EC 3.6.1.-) ; Kinesin (EC 3.6.4.4)
    Language English
    Publishing date 2017-01-30
    Publishing country England
    Document type Journal Article ; Research Support, Non-U.S. Gov't
    ISSN 2041-1723
    ISSN (online) 2041-1723
    DOI 10.1038/ncomms14177
    Database MEDical Literature Analysis and Retrieval System OnLINE

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