start-ver=1.4 cd-journal=joma no-vol=34 cd-vols= no-issue=12 article-no= start-page=16449 end-page=16463 dt-received= dt-revised= dt-accepted= dt-pub-year=2020 dt-pub=20201017 dt-online= en-article= kn-article= en-subject= kn-subject= en-title= kn-title=Dynamin 1 is important for microtubule organization and stabilization in glomerular podocytes en-subtitle= kn-subtitle= en-abstract= kn-abstract=Dynamin 1 is a neuronal endocytic protein that participates in vesicle formation by scission of invaginated membranes. Dynamin 1 is also expressed in the kidney; however, its physiological significance to this organ remains unknown. Here, we show that dynamin 1 is crucial for microtubule organization and stabilization in glomerular podocytes. By immunofluorescence and immunoelectron microscopy, dynamin 1 was concentrated at microtubules at primary processes in rat podocytes. By immunofluorescence of differentiated mouse podocytes (MPCs), dynamin 1 was often colocalized with microtubule bundles, which radially arranged toward periphery of expanded podocyte. In dynamin 1-depleted MPCs by RNAi, alpha-tubulin showed a dispersed linear filament-like localization, and microtubule bundles were rarely observed. Furthermore, dynamin 1 depletion resulted in the formation of discontinuous, short acetylated alpha-tubulin fragments, and the decrease of microtubule-rich protrusions. Dynamins 1 and 2 double-knockout podocytes showed dispersed acetylated alpha-tubulin and rare protrusions. In vitro, dynamin 1 polymerized around microtubules and cross-linked them into bundles, and increased their resistance to the disassembly-inducing reagents Ca(2+)and podophyllotoxin. In addition, overexpression and depletion of dynamin 1 in MPCs increased and decreased the nocodazole resistance of microtubules, respectively. These results suggest that dynamin 1 supports the microtubule bundle formation and participates in the stabilization of microtubules. en-copyright= kn-copyright= en-aut-name=LaThe Mon en-aut-sei=La en-aut-mei=The Mon kn-aut-name= kn-aut-sei= kn-aut-mei= aut-affil-num=1 ORCID= en-aut-name=TachibanaHiromi en-aut-sei=Tachibana en-aut-mei=Hiromi kn-aut-name= kn-aut-sei= kn-aut-mei= aut-affil-num=2 ORCID= en-aut-name=LiShun-Ai en-aut-sei=Li en-aut-mei=Shun-Ai kn-aut-name= kn-aut-sei= kn-aut-mei= aut-affil-num=3 ORCID= en-aut-name=AbeTadashi en-aut-sei=Abe en-aut-mei=Tadashi kn-aut-name= kn-aut-sei= kn-aut-mei= aut-affil-num=4 ORCID= en-aut-name=SeirikiSayaka en-aut-sei=Seiriki en-aut-mei=Sayaka kn-aut-name= kn-aut-sei= kn-aut-mei= aut-affil-num=5 ORCID= en-aut-name=NagaokaHikaru en-aut-sei=Nagaoka en-aut-mei=Hikaru kn-aut-name= kn-aut-sei= kn-aut-mei= aut-affil-num=6 ORCID= en-aut-name=TakashimaEizo en-aut-sei=Takashima en-aut-mei=Eizo kn-aut-name= kn-aut-sei= kn-aut-mei= aut-affil-num=7 ORCID= en-aut-name=TakedaTetsuya en-aut-sei=Takeda en-aut-mei=Tetsuya kn-aut-name= kn-aut-sei= kn-aut-mei= aut-affil-num=8 ORCID= en-aut-name=OgawaDaisuke en-aut-sei=Ogawa en-aut-mei=Daisuke kn-aut-name= kn-aut-sei= kn-aut-mei= aut-affil-num=9 ORCID= en-aut-name=MakinoShin-Ichi en-aut-sei=Makino en-aut-mei=Shin-Ichi kn-aut-name= kn-aut-sei= kn-aut-mei= aut-affil-num=10 ORCID= en-aut-name=AsanumaKatsuhiko en-aut-sei=Asanuma en-aut-mei=Katsuhiko kn-aut-name= kn-aut-sei= kn-aut-mei= aut-affil-num=11 ORCID= en-aut-name=WatanabeMasami en-aut-sei=Watanabe en-aut-mei=Masami kn-aut-name= kn-aut-sei= kn-aut-mei= aut-affil-num=12 ORCID= en-aut-name=TianXuefei en-aut-sei=Tian en-aut-mei=Xuefei kn-aut-name= kn-aut-sei= kn-aut-mei= aut-affil-num=13 ORCID= en-aut-name=IshibeShuta en-aut-sei=Ishibe en-aut-mei=Shuta kn-aut-name= kn-aut-sei= kn-aut-mei= aut-affil-num=14 ORCID= en-aut-name=SakaneAyuko en-aut-sei=Sakane en-aut-mei=Ayuko kn-aut-name= kn-aut-sei= kn-aut-mei= aut-affil-num=15 ORCID= en-aut-name=SasakiTakuya en-aut-sei=Sasaki en-aut-mei=Takuya kn-aut-name= kn-aut-sei= kn-aut-mei= aut-affil-num=16 ORCID= en-aut-name=WadaJun en-aut-sei=Wada en-aut-mei=Jun kn-aut-name= kn-aut-sei= kn-aut-mei= aut-affil-num=17 ORCID= en-aut-name=TakeiKohji en-aut-sei=Takei en-aut-mei=Kohji kn-aut-name= kn-aut-sei= kn-aut-mei= aut-affil-num=18 ORCID= en-aut-name=YamadaHiroshi en-aut-sei=Yamada en-aut-mei=Hiroshi kn-aut-name= kn-aut-sei= kn-aut-mei= aut-affil-num=19 ORCID= affil-num=1 en-affil=Department of Neuroscience, Graduate School of Medicine, Dentistry and Pharmaceutical Sciences, Okayama University kn-affil= affil-num=2 en-affil=Department of Nephrology, Rheumatology, Endocrinology and Metabolism, Graduate School of Medicine, Dentistry and Pharmaceutical Sciences, Okayama University kn-affil= affil-num=3 en-affil=Center for Innovative Clinical Medicine, Okayama University Hospital kn-affil= affil-num=4 en-affil=Department of Neuroscience, Graduate School of Medicine, Dentistry and Pharmaceutical Sciences, Okayama University kn-affil= affil-num=5 en-affil=Department of Neuroscience, Graduate School of Medicine, Dentistry and Pharmaceutical Sciences, Okayama University kn-affil= affil-num=6 en-affil=Division of Malaria Research, Proteo-Science Center, Ehime University kn-affil= affil-num=7 en-affil=Division of Malaria Research, Proteo-Science Center, Ehime University kn-affil= affil-num=8 en-affil=Department of Neuroscience, Graduate School of Medicine, Dentistry and Pharmaceutical Sciences, Okayama University kn-affil= affil-num=9 en-affil=Department of Nephrology, Rheumatology, Endocrinology and Metabolism, Graduate School of Medicine, Dentistry and Pharmaceutical Sciences, Okayama University kn-affil= affil-num=10 en-affil=Department of Nephrology, Graduate School of Medicine, Chiba University kn-affil= affil-num=11 en-affil=Department of Nephrology, Graduate School of Medicine, Chiba University kn-affil= affil-num=12 en-affil=Center for Innovative Clinical Medicine, Okayama University Hospital kn-affil= affil-num=13 en-affil=Department of Internal Medicine, Section of Nephrology, Yale University School of Medicine kn-affil= affil-num=14 en-affil=Department of Internal Medicine, Section of Nephrology, Yale University School of Medicine kn-affil= affil-num=15 en-affil=Department of Biochemistry, Tokushima University Graduate School of Medical Sciences kn-affil= affil-num=16 en-affil=Department of Biochemistry, Tokushima University Graduate School of Medical Sciences kn-affil= affil-num=17 en-affil=Department of Nephrology, Rheumatology, Endocrinology and Metabolism, Graduate School of Medicine, Dentistry and Pharmaceutical Sciences, Okayama University kn-affil= affil-num=18 en-affil=Department of Neuroscience, Graduate School of Medicine, Dentistry and Pharmaceutical Sciences, Okayama University kn-affil= affil-num=19 en-affil=Department of Neuroscience, Graduate School of Medicine, Dentistry and Pharmaceutical Sciences, Okayama University kn-affil= en-keyword=dynamin kn-keyword=dynamin en-keyword=microtubules kn-keyword=microtubules en-keyword=podocyte kn-keyword=podocyte en-keyword=primary process kn-keyword=primary process END start-ver=1.4 cd-journal=joma no-vol=49 cd-vols= no-issue=3 article-no= start-page=877 end-page=886 dt-received= dt-revised= dt-accepted= dt-pub-year=2016 dt-pub=20160630 dt-online= en-article= kn-article= en-subject= kn-subject= en-title= kn-title=Actin bundling by dynamin 2 and cortactin is implicated in cell migration by stabilizing filopodia in human non-small cell lung carcinoma cells en-subtitle= kn-subtitle= en-abstract= kn-abstract= The endocytic protein dynamin participates in the formation of actin-based membrane protrusions such as podosomes, pseudopodia, and invadopodia, which facilitate cancer cell migration, invasion, and metastasis. However, the role of dynamin in the formation of actin-based membrane protrusions at the leading edge of cancer cells is unclear. In this study, we demonstrate that the ubiquitously expressed dynamin 2 isoform facilitates cell migration by stabilizing F-actin bundles in filopodia of the lung cancer cell line H1299. Pharmacological inhibition of dynamin 2 decreased cell migration and filopodial formation. Furthermore, dynamin 2 and cortactin mostly colocalized along F-actin bundles in filopodia of serum-stimulated H1299 cells by immunofluorescent and immunoelectron microscopy. Knockdown of dynamin 2 or cortactin inhibited the formation of filopodia in serum-stimulated H1299 cells, concomitant with a loss of F-actin bundles. Expression of wild-type cortactin rescued the punctate-like localization of dynamin 2 and filopodial formation. The incubation of dynamin 2 and cortactin with F-actin induced the formation of long and thick actin bundles, with these proteins colocalizing at F-actin bundles. A depolymerization assay revealed that dynamin 2 and cortactin increased the stability of F-actin bundles. These results indicate that dynamin 2 and cortactin participate in cell migration by stabilizing F-actin bundles in filopodia. Taken together, these findings suggest that dynamin might be a possible molecular target for anticancer therapy. en-copyright= kn-copyright= en-aut-name=YamadaHiroshi en-aut-sei=Yamada en-aut-mei=Hiroshi kn-aut-name= kn-aut-sei= kn-aut-mei= aut-affil-num=1 ORCID= en-aut-name=TakedaTetsuya en-aut-sei=Takeda en-aut-mei=Tetsuya kn-aut-name= kn-aut-sei= kn-aut-mei= aut-affil-num=2 ORCID= en-aut-name=MichiueHiroyuki en-aut-sei=Michiue en-aut-mei=Hiroyuki kn-aut-name= kn-aut-sei= kn-aut-mei= aut-affil-num=3 ORCID= en-aut-name=AbeTadashi en-aut-sei=Abe en-aut-mei=Tadashi kn-aut-name= kn-aut-sei= kn-aut-mei= aut-affil-num=4 ORCID= en-aut-name=TakeiKohji en-aut-sei=Takei en-aut-mei=Kohji kn-aut-name= kn-aut-sei= kn-aut-mei= aut-affil-num=5 ORCID= affil-num=1 en-affil=Department of Neuroscience, Graduate School of Medicine, Dentistry and Pharmaceutical Sciences, Okayama University kn-affil= affil-num=2 en-affil=Department of Neuroscience, Graduate School of Medicine, Dentistry and Pharmaceutical Sciences, Okayama University kn-affil= affil-num=3 en-affil=Department of Physiology, Graduate School of Medicine, Dentistry and Pharmaceutical Sciences, Okayama University kn-affil= affil-num=4 en-affil=Department of Neuroscience, Graduate School of Medicine, Dentistry and Pharmaceutical Sciences, Okayama University kn-affil= affil-num=5 en-affil=Department of Neuroscience, Graduate School of Medicine, Dentistry and Pharmaceutical Sciences, Okayama University kn-affil= END start-ver=1.4 cd-journal=joma no-vol=123 cd-vols= no-issue=1 article-no= start-page=1 end-page=11 dt-received= dt-revised= dt-accepted= dt-pub-year=2011 dt-pub=20110401 dt-online= en-article= kn-article= en-subject= kn-subject= en-title=Dynamic interaction of amphiphysin with N-WASP regulates actin assembly kn-title=ƒAƒ“ƒtƒBƒtƒ@ƒCƒWƒ“‚ΖN-WASP‚Μƒ_ƒCƒiƒ~ƒbƒN‚Θ‘ŠŒέμ—p‚́CƒAƒNƒ`ƒ“d‡‚π§Œδ‚·‚ι en-subtitle= kn-subtitle= en-abstract= kn-abstract= en-copyright= kn-copyright= en-aut-name=YamadaHiroshi en-aut-sei=Yamada en-aut-mei=Hiroshi kn-aut-name=ŽR“c_Ži kn-aut-sei=ŽR“c kn-aut-mei=_Ži aut-affil-num=1 ORCID= en-aut-name=Padilla-ParraSergi en-aut-sei=Padilla-Parra en-aut-mei=Sergi kn-aut-name= kn-aut-sei= kn-aut-mei= aut-affil-num=2 ORCID= en-aut-name=ParkSun Joo en-aut-sei=Park en-aut-mei=Sun Joo kn-aut-name=–pι‘t kn-aut-sei=–p kn-aut-mei=ι‘t aut-affil-num=3 ORCID= en-aut-name=ItohToshiki en-aut-sei=Itoh en-aut-mei=Toshiki kn-aut-name=ˆΙ“‘rŽχ kn-aut-sei=ˆΙ“‘ kn-aut-mei=rŽχ aut-affil-num=4 ORCID= en-aut-name=ChaineauMathilde en-aut-sei=Chaineau en-aut-mei=Mathilde kn-aut-name= kn-aut-sei= kn-aut-mei= aut-affil-num=5 ORCID= en-aut-name=MonaldiIlaria en-aut-sei=Monaldi en-aut-mei=Ilaria kn-aut-name= kn-aut-sei= kn-aut-mei= aut-affil-num=6 ORCID= en-aut-name=CremonaOttavio en-aut-sei=Cremona en-aut-mei=Ottavio kn-aut-name= kn-aut-sei= kn-aut-mei= aut-affil-num=7 ORCID= en-aut-name=BenfenatiFabio en-aut-sei=Benfenati en-aut-mei=Fabio kn-aut-name= kn-aut-sei= kn-aut-mei= aut-affil-num=8 ORCID= en-aut-name=CamilliPietro De en-aut-sei=Camilli en-aut-mei=Pietro De kn-aut-name= kn-aut-sei= kn-aut-mei= aut-affil-num=9 ORCID= en-aut-name=Coppey-MoisanMa?t? en-aut-sei=Coppey-Moisan en-aut-mei=Ma?t? kn-aut-name= kn-aut-sei= kn-aut-mei= aut-affil-num=10 ORCID= en-aut-name=TramierMarc en-aut-sei=Tramier en-aut-mei=Marc kn-aut-name= kn-aut-sei= kn-aut-mei= aut-affil-num=11 ORCID= en-aut-name=GalliThierry en-aut-sei=Galli en-aut-mei=Thierry kn-aut-name= kn-aut-sei= kn-aut-mei= aut-affil-num=12 ORCID= en-aut-name=TakeiKohji en-aut-sei=Takei en-aut-mei=Kohji kn-aut-name=’|‹F“ρ kn-aut-sei=’|‹ kn-aut-mei=F“ρ aut-affil-num=13 ORCID= affil-num=1 en-affil= kn-affil=‰ͺŽR‘εŠw‘εŠw‰@ˆγŽ•–ςŠw‘‡Œ€‹†‰Θ@Ά‰»Šw affil-num=2 en-affil= kn-affil=ƒWƒƒƒbƒNƒ‚ƒmŒ€‹†Š affil-num=3 en-affil= kn-affil=_ŒΛ‘εŠw‘εŠw‰@ˆγŠwŒ€‹†‰Θ@–ŒΆ‰»Šw affil-num=4 en-affil= kn-affil=_ŒΛ‘εŠw‘εŠw‰@ˆγŠwŒ€‹†‰Θ@–ŒΆ•¨Šw affil-num=5 en-affil= kn-affil=ƒWƒƒƒbƒNƒ‚ƒmŒ€‹†Š affil-num=6 en-affil= kn-affil=ƒWƒFƒmƒo‘εŠw@ŽΐŒ±ˆγŠwC‘—§”]_Œo‰ΘŠwŒ€‹†ŠCƒCƒ^ƒŠƒAH‹ΖŒ€‹†Š@_Œo‰ΘŠwE”]HŠw affil-num=7 en-affil= kn-affil=‘—§_Œo‰ΘŠwŒ€‹†ŠCUniversitafVita-Salute San Raffaele •ͺŽqŽξα‡ŠwŒ€‹†Š affil-num=8 en-affil= kn-affil=ƒWƒFƒmƒo‘εŠw@ŽΐŒ±ˆγŠwC‘—§”]_Œo‰ΘŠwŒ€‹†ŠCƒCƒ^ƒŠƒAH‹ΖŒ€‹†Š@_Œo‰ΘŠwE”]HŠw affil-num=9 en-affil= kn-affil=ƒG[ƒ‹‘εŠwˆγŠw•”@Χ–EΆ•¨ŠwE_ŒoΆ•¨Šw affil-num=10 en-affil= kn-affil=ƒWƒƒƒbƒNƒ‚ƒmŒ€‹†Š affil-num=11 en-affil= kn-affil=ƒWƒƒƒbƒNƒ‚ƒmŒ€‹†Š affil-num=12 en-affil= kn-affil=ƒWƒƒƒbƒNƒ‚ƒmŒ€‹†Š affil-num=13 en-affil= kn-affil=‰ͺŽR‘εŠw‘εŠw‰@ˆγŽ•–ςŠw‘‡Œ€‹†‰Θ@Ά‰»Šw en-keyword=ƒAƒNƒ`ƒ“Χ–EœŠi kn-keyword=ƒAƒNƒ`ƒ“Χ–EœŠi en-keyword=ƒVƒiƒvƒX kn-keyword=ƒVƒiƒvƒX en-keyword=ƒGƒ“ƒhƒTƒCƒg[ƒVƒX kn-keyword=ƒGƒ“ƒhƒTƒCƒg[ƒVƒX en-keyword=ƒAƒ“ƒtƒBƒtƒ@ƒCƒWƒ“ kn-keyword=ƒAƒ“ƒtƒBƒtƒ@ƒCƒWƒ“ END start-ver=1.4 cd-journal=joma no-vol=203 cd-vols= no-issue=1 article-no= start-page=117 end-page=125 dt-received= dt-revised= dt-accepted= dt-pub-year=2001 dt-pub=200101 dt-online= en-article= kn-article= en-subject= kn-subject= en-title= kn-title=Synaptic-like microvesicles, synaptic vesicle counterparts in endocrine cells, are involved in a novel regulatory mechanism for the synthesis and secretion of hormones en-subtitle= kn-subtitle= en-abstract= kn-abstract=Microvesicles in endocrine cells are the morphological and functional equivalent of neuronal synaptic vesicles. Microvesicles accumulate various neurotransmitters through a transmitter-specific vesicular transporter energized by vacuolar H+-ATPase. We found that mammalian pinealocytes, endocrine cells that synthesize and secrete melatonin, accumulate L-glutamate in their microvesicles and secrete it through exocytosis. Pinealocytes use L-glutamate as either a paracrine- or autocrine-like chemical transmitter in a receptor-mediated manner, resulting in inhibition of melatonin synthesis. In this article, we briefly describe the overall features of the microvesicle-mediated signal-transduction mechanism in the pineal gland and discuss the important role of acidic organelles in a novel regulatory mechanism for hormonal synthesis and secretion. en-copyright= kn-copyright= en-aut-name=MoriyamaYoshinori en-aut-sei=Moriyama en-aut-mei=Yoshinori kn-aut-name= kn-aut-sei= kn-aut-mei= aut-affil-num=1 ORCID= en-aut-name=HayashiMitsuko en-aut-sei=Hayashi en-aut-mei=Mitsuko kn-aut-name= kn-aut-sei= kn-aut-mei= aut-affil-num=2 ORCID= en-aut-name=YamadaHiroshi en-aut-sei=Yamada en-aut-mei=Hiroshi kn-aut-name= kn-aut-sei= kn-aut-mei= aut-affil-num=3 ORCID= en-aut-name=YatsushiroShouki en-aut-sei=Yatsushiro en-aut-mei=Shouki kn-aut-name= kn-aut-sei= kn-aut-mei= aut-affil-num=4 ORCID= en-aut-name=IshioShougo en-aut-sei=Ishio en-aut-mei=Shougo kn-aut-name= kn-aut-sei= kn-aut-mei= aut-affil-num=5 ORCID= en-aut-name=YamamotoAkitsugu en-aut-sei=Yamamoto en-aut-mei=Akitsugu kn-aut-name= kn-aut-sei= kn-aut-mei= aut-affil-num=6 ORCID= affil-num=1 en-affil= kn-affil=Department of Biochemistry, Faculty of Pharmaceutical Sciences, Okayama University affil-num=2 en-affil= kn-affil=Department of Biochemistry, Faculty of Pharmaceutical Sciences, Okayama University affil-num=3 en-affil= kn-affil=Department of Biochemistry, Faculty of Pharmaceutical Sciences, Okayama University affil-num=4 en-affil= kn-affil=Department of Biochemistry, Faculty of Pharmaceutical Sciences, Okayama University affil-num=5 en-affil= kn-affil=Department of Biochemistry, Faculty of Pharmaceutical Sciences, Okayama University affil-num=6 en-affil= kn-affil=Department of Physiology, Kansai Medical University en-keyword=V-ATPase kn-keyword=V-ATPase en-keyword=melatonin kn-keyword=melatonin en-keyword=L-glutamate kn-keyword=L-glutamate en-keyword=serotonin kn-keyword=serotonin en-keyword=paracrine kn-keyword=paracrine en-keyword=autocrine kn-keyword=autocrine en-keyword=pinealocyte kn-keyword=pinealocyte en-keyword=endocrine cell. kn-keyword=endocrine cell. END start-ver=1.4 cd-journal=joma no-vol=62 cd-vols= no-issue=6 article-no= start-page=385 end-page=391 dt-received= dt-revised= dt-accepted= dt-pub-year=2008 dt-pub=200812 dt-online= en-article= kn-article= en-subject= kn-subject= en-title= kn-title=Dynamin 2 Cooperates with Amphiphysin 1 in Phagocytosis in Sertoli Cells en-subtitle= kn-subtitle= en-abstract= kn-abstract=

Testicular Sertoli cells highly express dynamin 2 and amphiphysin 1. Here we demonstrate that dynamin 2 is implicated in phosphatidylserine (PS)-dependent phagocytosis in Sertoli cells. Immunofluorescence and dual-live imaging revealed that dynamin 2 and amphiphysin 1 accumulate simultaneously at ruffles. These proteins are specifically bound in vitro. Over-expression of dominant negative dynamin 2 (K44A) inhibits liposome-uptake and leads to the mis-localization of amphiphysin 1. Thus, the cooperative function of dynamin 2 and amphiphysin 1 in PS-dependent phagocytosis is strongly suggested.

en-copyright= kn-copyright= en-aut-name=NakanishiAkira en-aut-sei=Nakanishi en-aut-mei=Akira kn-aut-name= kn-aut-sei= kn-aut-mei= aut-affil-num=1 ORCID= en-aut-name=AbeTadashi en-aut-sei=Abe en-aut-mei=Tadashi kn-aut-name= kn-aut-sei= kn-aut-mei= aut-affil-num=2 ORCID= en-aut-name=WatanabeMasami en-aut-sei=Watanabe en-aut-mei=Masami kn-aut-name= kn-aut-sei= kn-aut-mei= aut-affil-num=3 ORCID= en-aut-name=TakeiKohji en-aut-sei=Takei en-aut-mei=Kohji kn-aut-name= kn-aut-sei= kn-aut-mei= aut-affil-num=4 ORCID= en-aut-name=YamadaHiroshi en-aut-sei=Yamada en-aut-mei=Hiroshi kn-aut-name= kn-aut-sei= kn-aut-mei= aut-affil-num=5 ORCID= affil-num=1 en-affil= kn-affil=Department of Neuroscience, Okayama University Graduate School of Medicine, Dentistry and Pharmaceutical Sciences affil-num=2 en-affil= kn-affil=Department of Neuroscience, Okayama University Graduate School of Medicine, Dentistry and Pharmaceutical Sciences affil-num=3 en-affil= kn-affil=Department of Urology, Okayama University Graduate School of Medicine, Dentistry and Pharmaceutical Sciences affil-num=4 en-affil= kn-affil=Department of Neuroscience, Okayama University Graduate School of Medicine, Dentistry and Pharmaceutical Sciences affil-num=5 en-affil= kn-affil=Department of Neuroscience, Okayama University Graduate School of Medicine, Dentistry and Pharmaceutical Sciences en-keyword=dynamin kn-keyword=dynamin en-keyword=amphiphysin kn-keyword=amphiphysin en-keyword=phagocytosis kn-keyword=phagocytosis en-keyword=testis kn-keyword=testis END