Krishna Mudumbi, Ph.D.

Assistant Professor

krishna.mudumbi@vanderbilt.edu
Faculty Appointments
Assistant Professor of Cell & Developmental Biology
Education
Ph.D., Molecular and Cellular Biology, Temple University, Philadelphia, Pennsylvania
Clinical Description
The Mudumbi lab studies signal transduction and focuses on 2 main areas of research: 1) receptor activation kinetics and 2) downstream signaling kinetics. By understanding the kinetics of signal transduction from the level of both receptor signaling and downstream events, we hope to build a ‘kinetic landscape’ to understand how receptors achieve distinct signaling responses through the same receptor – a phenomenon known as biased signaling. This will allow us to target these kinetics with therapeutics and modulate or ‘fine-tune’ them for specific cellular outcomes in the future.

To understand the mechanisms of receptor mediated signaling, the Mudumbi lab combines cutting-edge live cell imaging techniques – single-particle tracking (SPT), single-molecule Förster resonance energy transfer (smFRET), super-resolution microscopy, and single-cell FRET to name a few – with a number of other biochemical and molecular biology approaches (phosphoproteomics, signaling assays, etc)
Clinical Research Keywords
Cell signaling, receptor tyrosine kinases, membrane proteins, single-molecule microscopy, super-resolution microscopy, biophysics, cancer
Publications
Mudumbi KC, Burns EA, Schodt DJ, Petrova ZO, Kiyatkin A, Kim LW, Mangiacapre EM, Ortiz-Caraveo I, Rivera Ortiz H, Hu C, Ashtekar KD, Lidke KA, Lidke DS, Lemmon MA. Distinct interactions stabilize EGFR dimers and higher-order oligomers in cell membranes. Cell Rep [print-electronic]. 2024 Jan 1/23/2024; 43(1): 113603. PMID: 38117650, PMCID: PMC10835193, PII: S2211-1247(23)01615-7, DOI: 10.1016/j.celrep.2023.113603, ISSN: 2211-1247.

Mudumbi KC, Burns EA, Schodt DJ, Petrova ZO, Kiyatkin A, Kim LW, Mangiacapre EM, Ortiz-Caraveo I, Ortiz HR, Hu C, Ashtekar KD, Lidke KA, Lidke DS, Lemmon MA. Distinct interactions stabilize EGFR dimers and higher-order oligomers in cell membranes. BioRxiv. 2023 Apr 4/10/2023; PMID: 37090557, PMCID: PMC10120646, PII: 2023.04.10.536273, DOI: 10.1101/2023.04.10.536273, ISSN: 2692-8205.

Li T, Stayrook SE, Tsutsui Y, Zhang J, Wang Y, Li H, Proffitt A, Krimmer SG, Ahmed M, Belliveau O, Walker IX, Mudumbi KC, Suzuki Y, Lax I, Alvarado D, Lemmon MA, Schlessinger J, Klein DE. Structural basis for ligand reception by anaplastic lymphoma kinase. Nature [print-electronic]. 2021 Dec; 600(7887): 148-52. PMID: 34819665, PMCID: PMC8639777, PII: 10.1038/s41586-021-04141-7, DOI: 10.1038/s41586-021-04141-7, ISSN: 1476-4687.

Mudumbi KC, Czapiewski R, Ruba A, Junod SL, Li Y, Luo W, Ngo C, Ospina V, Schirmer EC, Yang W. Nucleoplasmic signals promote directed transmembrane protein import simultaneously via multiple channels of nuclear pores. Nat Commun. 2020 May 5/4/2020; 11(1): 2184. PMID: 32366843, PMCID: PMC7198523, PII: 10.1038/s41467-020-16033-x, DOI: 10.1038/s41467-020-16033-x, ISSN: 2041-1723.

Tingey M, Mudumbi KC, Schirmer EC, Yang W. Casting a Wider Net: Differentiating between Inner Nuclear Envelope and Outer Nuclear Envelope Transmembrane Proteins. Int J Mol Sci. 2019 Oct 10/23/2019; 20(21): PMID: 31652739, PMCID: PMC6862087, PII: ijms20215248, DOI: 10.3390/ijms20215248, ISSN: 1422-0067.

Mudumbi KC, Yang W. Determination of Membrane Protein Distribution on the Nuclear Envelope by Single-Point Single-Molecule FRAP. Curr Protoc Cell Biol. 2017 Sep 9/1/2017; 76: 21.11.1-21.11.13-21.11.13. PMID: 28862339, PMCID: PMC5879780, DOI: 10.1002/cpcb.27, ISSN: 1934-2616.

Mudumbi KC, Schirmer EC, Yang W. Single-point single-molecule FRAP distinguishes inner and outer nuclear membrane protein distribution. Nat Commun. 2016 Aug 8/25/2016; 7: 12562. PMID: 27558844, PMCID: PMC5007294, PII: ncomms12562, DOI: 10.1038/ncomms12562, ISSN: 2041-1723.

Mudumbi KC, Yang W. Probing Protein Distribution Along the Nuclear Envelope In Vivo by Using Single-Point FRAP. Methods Mol Biol. 2016; 1411: 113-22. PMID: 27147037, PMCID: PMC10099394, DOI: 10.1007/978-1-4939-3530-7_6, ISSN: 1940-6029.

Mudumbi KC, Julius A, Herrmann J, Li E. The pathogenic A391E mutation in FGFR3 induces a structural change in the transmembrane domain dimer. J Membr Biol [print-electronic]. 2013 Jun; 246(6): 487-93. PMID: 23727984, DOI: 10.1007/s00232-013-9563-6, ISSN: 1432-1424.