607-255-0667
fh87@cornell.edu
345 Weill Hall
Research Scientist
Publications | Research | Faculty
Background:
Fenghua Hu is a research scientist in the Department of Molecular Biology and Genetics and is a member of the Weill Institute for Cell and Molecular Biology (Weill Institute). She received her B.S. in Biochemistry from Peking University in China in 1997 and her Ph.D. from Baylor College of Medicine in 2002. She received her postdoctoral training at Yale University, where she was awarded a Postdoctoral Fellowship from Paralyzed Veteran of American foundation.
Neurons in the mammalian peripheral nervous system (PNS) can regrow functional axons after injury but neurons from adult mammalian central nervous system (CNS) cannot. The ability of neurons to regenerate is determined by both the surrounding environment and factors intrinsic to the damaged neuron. Multiple inhibitors of axon regeneration have been identified in the CNS myelin during the past few years, including Nogo-A, myelin-associated glycoprotein (MAG), oligodendrocyte-myelin glycoprotein (OMGP) and chondroitin sulfate proteoglycan (CSPG). A group of regeneration associated genes gets upregulated to facilitate regeneration during successful regeneration in the PNS but is absent in CNS. Understanding the molecules and signaling pathways regulating axon outgrowth and regeneration will greatly facilitate drug design to promote axon regeneration and recovery after CNS injury. My laboratory is interested in dissecting the signaling pathways involved in myelin inhibition and identifying novel factors and pathways involved in successful axon regeneration using molecular and genomic tools.
Another area of interest is mechanisms involved neurodegeneration, particularly the function of progranulin in the CNS and its relevance to frontotemporal dementia. Progranulin is a secreted glycoprotein involved in wound healing, inflammation and tumorigenesis. Mutations in progranulin are found in patients with frontotemporal dementia, although its function in CNS is largely unknown. My laboratory is interested in elucidating functions of progranulin in the CNS and the receptor(s) and signaling pathways involved in these processes.
Publications:
The N-Terminal Domain of Nogo-A Inhibits Cell Adhesion and Axonal Outgrowth by an Integrin-Specific Mechanism. J Neurosci. 2008 Jan 30;28(5):1262-9
2. Laurén J, Hu F, Chin J, Liao J, Airaksinen MS and Strittmatter SM
Complex ligand-receptor interactions of myelin inhibitors of axon growth with Nogo-66 receptor family members. J Biol Chem. 2007 Feb 23;282(8):5715-25
3. Miao RQ, Gao Y, Harrison KD, Prendergast J, Acevedo LM, Yu J, Hu F, Strittmatter SM, Sessa WC.
Identification of a receptor necessary for Nogo-B stimulated chemotaxis and morphogenesis of endothelial cells. Proc Natl Acad Sci U S A. 2006 Jul 18;103(29):10997-1002.
4. Hu F, Liu B, Budel S, Chin J, Liao J, Fournier A and Strittmatter SM.
Nogo-A interacts with the Nogo-66 receptor through multiple sites to create an isoform-selective subnanomolar agonist. J Neurosci. 2005 Jun 1;25(22):5298-304
5. Hu F and Strittmatter SM.
Regulating axon growth within the postnatal central nervous system. Semin Perinatol. 2004 Dec;28(6):371-8.
6. Hu F, Elledge SJ.
Bub2 is a cell cycle regulated phospho-protein controlled by multiple checkpoints. Cell Cycle. 2002 Sep-Oct;1(5):351-5.
7. Hu F*, Y. Wang*, D. Liu, Y.Li, J. Qin and Elledge SJ.
Regulation of Bfa1 by Cdc5 and cell cycle checkpoints. Cell 2001 Nov 30;107:655-665
8. Alcasabas AA, Osborn AJ*, Bachant J*, Hu F*, Werler PJ, Bousset K, Furuya K, Diffley JF, Carr A, and Elledge SJ.
Mrc1 transduces signals of DNA replication stress to activate Rad53. Nat. Cell. Biol. 2001 Nov 1;3:958-965
9. Hu F, Alcasabas AA and Elledge SJ.
Asf1 links Rad53 to control of chromatin assembly. Genes Dev. 2001 May 1;15(9):1061-6.
10. Wang Y*, Hu F* and Elledge SJ.
The Bfa1/Bub2 GAP complex comprises a universal checkpoint required to prevent mitotic exit. Curr Biol. 2000 Nov 2;10(21):1379-82.
11. Sanchez Y, Bachant J, Wang H, Hu F, Liu D, Tetzlaff M and Elledge SJ.
Control of the DNA damage checkpoint by Chk1 and Rad53 protein kinases through distinct mechanisms. Science 1999 Nov 5;286(5442):1166-71.