EB1 is required for primary cilia assembly in fibroblasts.
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EB1 is required for primary cilia assembly in fibroblasts. / Schrøder, Jacob M; Schneider, Linda; Christensen, Søren T; Pedersen, Lotte B.
I: Current Biology, Bind 17, Nr. 13, 2007, s. 1134-9.Publikation: Bidrag til tidsskrift › Tidsskriftartikel › Forskning › fagfællebedømt
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T1 - EB1 is required for primary cilia assembly in fibroblasts.
AU - Schrøder, Jacob M
AU - Schneider, Linda
AU - Christensen, Søren T
AU - Pedersen, Lotte B
N1 - Keywords: Animals; Antigens; Cell Cycle; Centrioles; Cilia; Fibroblasts; Gene Expression; Green Fluorescent Proteins; Mice; Microtubule-Associated Proteins; NIH 3T3 Cells; RNA, Small Interfering
PY - 2007
Y1 - 2007
N2 - EB1 is a small microtubule (MT)-binding protein that associates preferentially with MT plus ends and plays a role in regulating MT dynamics. EB1 also targets other MT-associated proteins to the plus end and thereby regulates interactions of MTs with the cell cortex, mitotic kinetochores, and different cellular organelles [1, 2]. EB1 also localizes to centrosomes and is required for centrosomal MT anchoring and organization of the MT network [3, 4]. We previously showed that EB1 localizes to the flagellar tip and proximal region of the basal body in Chlamydomonas[5], but the function of EB1 in the cilium/flagellum is unknown. We depleted EB1 from NIH3T3 fibroblasts by using siRNA and found that EB1 depletion causes a approximately 50% reduction in the efficiency of primary cilia assembly in serum-starved cells. Expression of dominant-negative EB1 also inhibited cilia formation, and expression of mutant dominant-negative EB1 constructs suggested that binding of EB1 to p150(Glued) is important for cilia assembly. Finally, expression of a C-terminal fragment of the centrosomal protein CAP350, which removes EB1 from the centrosome but not MT plus ends [6], also inhibited ciliogenesis. We conclude that localization of EB1 at the centriole/basal body is required for primary cilia assembly in fibroblasts.
AB - EB1 is a small microtubule (MT)-binding protein that associates preferentially with MT plus ends and plays a role in regulating MT dynamics. EB1 also targets other MT-associated proteins to the plus end and thereby regulates interactions of MTs with the cell cortex, mitotic kinetochores, and different cellular organelles [1, 2]. EB1 also localizes to centrosomes and is required for centrosomal MT anchoring and organization of the MT network [3, 4]. We previously showed that EB1 localizes to the flagellar tip and proximal region of the basal body in Chlamydomonas[5], but the function of EB1 in the cilium/flagellum is unknown. We depleted EB1 from NIH3T3 fibroblasts by using siRNA and found that EB1 depletion causes a approximately 50% reduction in the efficiency of primary cilia assembly in serum-starved cells. Expression of dominant-negative EB1 also inhibited cilia formation, and expression of mutant dominant-negative EB1 constructs suggested that binding of EB1 to p150(Glued) is important for cilia assembly. Finally, expression of a C-terminal fragment of the centrosomal protein CAP350, which removes EB1 from the centrosome but not MT plus ends [6], also inhibited ciliogenesis. We conclude that localization of EB1 at the centriole/basal body is required for primary cilia assembly in fibroblasts.
U2 - 10.1016/j.cub.2007.05.055
DO - 10.1016/j.cub.2007.05.055
M3 - Journal article
C2 - 17600711
VL - 17
SP - 1134
EP - 1139
JO - Current Biology
JF - Current Biology
SN - 0960-9822
IS - 13
ER -
ID: 3799236