U.S. Department of Health and Human Services
Gregory Germino
 

 Contact Info

 
Tel: 301-496-5877
Email: germinogg@mail.nih.gov
 

 Select Experience

 
  • Senior InvestigatorKidney Diseases Branch, NIDDK, NIH2009–Present
  • Adjunct Professor of MedicineJohns Hopkins University School of Medicine2009–Present
  • Professor of Medicine Division of Nephrology, Johns Hopkins University School of Medicine2003–2009
  • Affiliate MemberMcKusick-Nathans Institute of Genetic Medicine, Johns Hopkins University School of Medicine2002–2009
  • Joint AppointmentDepartment of Molecular Biology and Genetics, Johns Hopkins University School of Medicine2001–2009
  • Associate Professor of MedicineDivision of Nephrology, Johns Hopkins University School of Medicine1997–2003
  • Assistant Professor of MedicineDivision of Nephrology, Johns Hopkins University School of Medicine1992–1997
  • Associate Research ScientistInstructor and Assistant Professor, Yale University School of Medicine1988–1992
  • Research Post-Doctoral FellowNuffield Department of Medicine, Oxford University1987–1988
  • Clinical Post-Doctoral FellowNephrology, Yale University School of Medicine1986–1987
  • Internal Medicine ResidencyYale–New Haven Hospital1983–1986
  • M.D.AOA, University of Chicago Pritzker School of Medicine1983
  • B.S.Loyola University of Chicago1979
 

 Related Links

 

Gregory G. Germino, M.D.

Deputy Director​, Office of the Director​
Chief, Kidney Diseases Branch, Polycystic Kidney Disease Laboratory

Specialties: Molecular Biology/Biochemistry, Genetics/Genomics, Nephrology​​

Gregory Germino

Chief, Kidney Diseases BranchPolycystic Kidney Disease Laboratory
Deputy Director, Office of the Director
Deputy Director, Office of the Deputy Director
Acting Director, Technology Advancement Office
Specialties
  • Genetics/Genomics
  • Molecular Biology/Biochemistry
  • Nephrology

​Research Images

Images or videos appear below. Clicking images or videos provides an expanded view.

TitleDescriptionImage
Normal adult mouse kidneyTop: Normal adult mouse kidney stained with markers that distinguish proximal (green) and distal tubules (red). The image highlights the complex tubular structure of the kidney. (Cover, Nat Med Vol. 13, December 2007; Piontek et al, same issue 1490-1495). Bottom: Immunofluorescent image of a cystic mouse kidney stained for tubular markers.Normal adult mouse kidneyEnlarge
Human cystic kidneyA human cystic kidney removed from an individual with autosomal dominant polycystic kidney disease is depicted. For comparison, a normal adult kidney is approximately the size of a human fist.Human cystic kidneyEnlarge
Polycystin-1 (PC1) and Polycystin-2 (PC2) form a receptor-channel complex at the cell membraneTop: The lab has previously shown that the PKD1 and PKD2 gene products form a heteromeric complex at the cell membrane. Our group is focused on identifying what the complex senses and how it signals its response. (Qian et al, Nat Genet 16: 179-183, 1997; Hanoaka et al, Nature 408: 990-994, 2000). Bottom: Numerous proteins associated with cystic kidneys (‘‘cystoproteins’’) localize to the primary cilium and basal body complex but are also found in other intracellular compartments. AJ, adherens junction; BB, basal body; Cen, centriole; ER, endoplasmic reticulum; FAP, focal adhesion plaque; TJ, tight junction. (Menezes et al, Methods Cell Biol 94:273-297, 2009).Polycystin-1 (PC1) and Polycystin-2 (PC2) form a receptor-channel complex at the cell membraneEnlarge
Non-canonical Wnt signaling and tubular morphogenesisPlanar cell polarity might be involved in the establishment of normal tubular architecture in several different ways, including directional cell division, preservation of cellular spatial orientation information, and/or convergent extension/directional cell migration. Disruption of any of these processes could potentially result in cyst formation (Germino GG. Nature Genet, 37:455-457, 2005; Menezes et al, Methods Cell Biol 94:273-297, 2009).Non-canonical Wnt signaling and tubular morphogenesisEnlarge
Polyductin undergoes Notch-1 like processingThe laboratory has shown that polyductin, the gene product encoded by the gene (PKHD1) mutated in human ARPKD, undergoes Notch-1 like post-translational processing with regulated shedding of an ectodomain and release of an intracellular C-terminal (Cover, Hum Mol Genet Vol 16, April 2007; Kaimori et al, same issue, pp942-956)Polyductin undergoes Notch-1 like processingEnlarge