Lab Members
Rout, Michael P.
Professor
Laboratory of Cellular and Structural Biology
E-mail: Michael.Rout@rockefeller.edu
Aitchison, John
Member of the Adjunct Faculty
E-mail: John.Aitchison@rockefeller.edu
Fernandez Martinez, Javier
Research Associate
E-mail: Javier.FernandezMartinez@rockefeller.edu
Field, Mark
Visiting Professor
E-mail: Mark.Field@rockefeller.edu
Fridy, Peter
Graduate Fellow
E-mail: Peter.Fridy@rockefeller.edu
Hakhverdyan, Zhanna
Graduate Fellow
E-mail: Zhanna.Hakhverdyan@rockefeller.edu
Hatton, Beth Anne
Administrative Assistant
E-mail: bethanne.hatton@rockefeller.edu
Hayama, Ryo
Postdoctoral Associate
E-mail: Ryo.Hayama@rockefeller.edu
Hecht, Lee
Research Assistant
E-mail: Lee.Hecht@rockefeller.edu
Jiang, Hua
Scientific Project Coordinator
E-mail: Hua.Jiang@rockefeller.edu
Kaback, David
Visiting Professor
E-mail: David.Kaback@rockefeller.edu
Ketaren, Natalia
Research Associate
E-mail: Natalia.Ketaren@rockefeller.edu
Leung, Bic-Hang
Skilled Laboratory Helper
E-mail: Bic-Hang.Leung@rockefeller.edu
Lord, Oshane
Laboratory Helper
E-mail: Oshane.Lord@rockefeller.edu
Nudelman, Ilona
Research Associate
E-mail: Ilona.Nudelman@rockefeller.edu
Obado, Samson
Research Associate
E-mail: Samson.Obado@rockefeller.edu
Serganov, Artem
Graduate Fellow
E-mail: artem.serganov@rockefeller.edu
Simon, Dan
Postdoctoral Associate
E-mail: Dan.Simon@rockefeller.edu
Trivedi, Jill
Research Assistant
E-mail: Jill.Trivedi@rockefeller.edu
Udi, Yael
Postdoctoral Associate
E-mail: Yael.Udi@rockefeller.edu
Upla, Paula
Visiting Fellow
E-mail: Paula.Upla@rockefeller.edu
Williams, Rosemary
Laboratory Manager
E-mail: Rosemary.Williams@rockefeller.edu
LaCava, John
Research Assistant Professor
E-mail: John.LaCava@rockefeller.edu
LaCava Group - Lines of Investigation
Improving Methods and Technology for Interactome Analyses
Proteins and the macromolecular complexes they form are the effectors of cell biology. Studying cell biology therefore requires the ability to isolate distinct proteins along with other constituents of their associated complexes. Affinity capture techniques have greatly facilitated the discovery, purification, and characterization of endogenous macromolecular complexes. These techniques leverage reagents able to target and capture proteins of interest assembled with physiological binding partners, from cell extracts. Although these techniques have matured steadily, there remain a great number of challenges limiting the application of this approach to authentic retrieval of intact, bona fide physiological complexes. We develop mass spectrometry-based, affinity proteomics techniques for interactome mapping. We place special emphasis on approaches that also enable downstream structural and biochemical studies of purified macromolecular complexes.
Characterizing Human L1 Retrotransposons
Long Interspersed Nuclear Element 1 (L1) is a retrotransposon active in mammalian genomes. As a result of a "copy and paste" method of proliferation, L1 activity has contributed a large proportion of DNA to the human genome (including those sequences mobilized by L1, such as Alus). Since the insertion of new DNA sequences into the genome is inherently mutagenic, understanding the lifecycle of L1 is crucial to understanding human genome dynamics and cell biology. L1 DNA proliferates through an RNA intermediate whose protein products bind the L1 RNA to form a ribonucleoprotein (RNP) complex. L1 RNPs also coopt and contend with a variety of host factors that facilitate or repress L1's ability to reach the chromatin and reintegrate into the genome. Thus, different subpopulations of L1s consist of different assortments of constituents, depending both on the subcellular compartment and on the pathway being traversed (proliferation or repression). We develop methods to expand our breadth of knowledge concerning the L1 interactome, and we study the structural and biochemical properties of L1 RNPs.
Characterizing Human RNA Processing
The RNA exosome is a macromolecular complex comprising endo- and exoribonucleases. It is an essential component of the RNA-metabolism machinery in eukaryotes, functioning in the accurate processing of precursors to mature RNAs and in RNA turnover. The exosome is active in both the nucleus and the cytoplasm, and depending on the subcellular compartment where the exosome is active, the constituents of the complex and associated adapters vary - yielding a collection of distinctive subpopulations in vivo. We focus on the discovery, purification, and characterization of endogenous human exosomes and their cofactor complexes.
