Henry N. Higgs, PhD
Title(s)
Professor of Biochemistry and Cell Biology
John La Porte Given Foundation, Inc. Professorship in Cytology
Department(s)
Biochemistry and Cell Biology
Education
Lafayette College, BA 1987U. Washington, PHD 1996
Programs
Molecular and Cellular Biology Graduate Programs
Contact Information
Dartmouth Medical School
HB 7200
Hanover NH 03755
Professional Interests
Microvilli cover the surface of circulating blood lymphocytes. Lymphocytes use these finger-like projections to segregate adhesion receptors, as certain receptors localize to microvilli while others are excluded from them. Adhesion receptor segregation is crucial because cells use these receptors sequentially when moving from the bloodsteam to specific tissues. Little is known about the architecture of microvilli, nor about their relationship to similar structures from other cells. My lab will identify protein components crucial to microvillar structure, test how mutation of these proteins affect microvillar structure and function, and characterize how these proteins function biochemically and biophysically.
Selected Publications |
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Mitochondrial dysfunction triggers actin polymerization necessary for rapid glycolytic activation. Myosin II proteins are required for organization of calcium-induced actin networks upstream of mitochondrial division. Parallel kinase pathways stimulate actin polymerization at depolarized mitochondria. Mff oligomerization is required for Drp1 activation and synergy with actin filaments during mitochondrial division. Multiple roles for actin in secretory and endocytic pathways. SEC24A facilitates colocalization and Ca(2)(+) flux between the endoplasmic reticulum and mitochondria. Lysine acetylation of cytoskeletal proteins: Emergence of an actin code. Tumor microtubes connect pancreatic cancer cells in an Arp2/3 complex-dependent manner. FSGS-Causing INF2 Mutation Impairs Cleaved INF2 N-Fragment Functions in Podocytes. Regulation of INF2-mediated actin polymerization through site-specific lysine acetylation of actin itself. |
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