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Nathan E. Grega-Larson
Researcher at Vanderbilt University
Publications - 12
Citations - 1028
Nathan E. Grega-Larson is an academic researcher from Vanderbilt University. The author has contributed to research in topics: Brush border & Actin cytoskeleton. The author has an hindex of 10, co-authored 12 publications receiving 791 citations. Previous affiliations of Nathan E. Grega-Larson include Vanderbilt University Medical Center.
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Journal ArticleDOI
Exosome secretion is enhanced by invadopodia and drives invasive behavior.
Daisuke Hoshino,Kellye C. Kirkbride,Kaitlin Costello,Emily S. Clark,Seema Sinha,Nathan E. Grega-Larson,Matthew J. Tyska,Alissa M. Weaver +7 more
TL;DR: This work identified specialized invasive actin structures called invadopodia as specific and critical docking and secretion sites for CD63- and Rab27a-positive MVEs and revealed a fundamental role for exosomes in promoting cancer cell invasiveness.
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Cortactin promotes exosome secretion by controlling branched actin dynamics.
Seema Sinha,Daisuke Hoshino,Nan Hyung Hong,Kellye C. Kirkbride,Nathan E. Grega-Larson,Motoharu Seiki,Matthew J. Tyska,Alissa M. Weaver,Alissa M. Weaver +8 more
TL;DR: It is shown that the cytoskeletal and tumor-overexpressed protein cortactin promotes secretion of exosomes from cancer cells by stabilizing dynamic cortical actin docking sites for multivesicular endosomes, suggesting a potential mechanism by which Cortactin may promote tumor aggressiveness.
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Intestinal brush border assembly driven by protocadherin-based intermicrovillar adhesion.
Scott W. Crawley,David A. Shifrin,Nathan E. Grega-Larson,Russell E. McConnell,Andrew E. Benesh,Suli Mao,Yuxi Zheng,Qing Yin Zheng,Ki Taek Nam,Bryan A. Millis,Bechara Kachar,Matthew J. Tyska +11 more
TL;DR: It is found that brush border assembly is driven by the formation of Ca(2+)-dependent adhesion links between adjacent microvilli, and this discovery illuminate the basis of intestinal pathology in patients with Usher syndrome.
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ANKS4B Is Essential for Intermicrovillar Adhesion Complex Formation
TL;DR: This study uncovers an essential role for ANKS4B in brush border assembly, reveals a hierarchy in the molecular interactions that drive intermicrovillar adhesion, and informs the understanding of diseases caused by mutations in USH1C and ankyrin repeat proteins, such as Usher syndrome.
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IRTKS (BAIAP2L1) Elongates Epithelial Microvilli Using EPS8-Dependent and Independent Mechanisms
TL;DR: Report that the inverse-bin-amphiphysin-Rvs (I-BAR)-domain-containing protein insulin receptor tyrosine kinase substrate (IRTKS) promotes the growth of epithelial microvilli and explains why IRTKS is targeted by enteric pathogens that disrupt microvillar structure during infection of the intestinal epithelium.