Oocytes are life's time capsules. They can hibernate for days to decades before they experience a dramatic awakening, called activation. Once fertilized, these oocytes reprogram themselves to become a rapidly dividing embryo. How does an oocyte organize its cytoplasm to survive hibernation and protect itself against aging? How is the oocyte reorganized to promote rapid, mitotic divisions? What are the safeguards to prevent and correct errors in this crucial reprogramming?

Our mission is to understand the design principles of cytoplasmic reorganization during the oocyte-to-embryo transition.

Female mammals must store their oocytes over years to decades before they are ovulated. A decrease in oocyte quality over time is a major factor in age-related infertility. We study how the oocyte cytoplasm is reorganized to shut down cellular metabolism and protect its precious contents to survive long-term hibernation.

Biomolecular condensates in the germline

Oocytes and embryos compartmentalize their cytoplasm by building supramolecular assemblies of proteins and nucleic acids, termed "biomolecular condensates". We want to understand how these condensates control protein translation, metabolism, and cytoskeletal organization during the oocyte-to-embryo transition.

Principles of error-free cell division

After fertilization, the oocyte switches to mitotic cell divisions orchestrated by centrosomes, which are membrane-less organelles that nucleate and organize microtubules. Dysregulation of centrosome formation is lethal during embryogensis and can trigger tumor formation and metastasis in somatic cells. We want to understand how centrosomes assemble and nucleate microtubules through bottom-up reconstitution.

Meet the Woodruff Lab

Jeff Woodruff, PhD

Assistant Professor

Weronika Stachera

Grad Student

Nicole Familiari

Lab Manager

Jessica Alatorre

Research Assistant

Manolo Rios

Grad student

Matthew Amato

Grad Student

Priyankaa Bhatia

Grad student

Kan Yaguchi, PhD

Post-doc

Featured Publications

Regulated changes in material properties underlie centrosome disassembly during mitotic exit.

Mittasch M, Tran VM, Rios MU, Fritsch AW, Enos SJ, Ferreira Gomes B, Bond A, Kreysing M, Woodruff JB, 2020 Apr J. Cell Biol. 4 219

The Centrosome Is a Selective Condensate that Nucleates Microtubules by Concentrating Tubulin.

Woodruff JB, Ferreira Gomes B, Widlund PO, Mahamid J, Honigmann A, Hyman AA 2017 Jun Cell 6 169 1066-1077.e10

Centrosomes. Regulated assembly of a supramolecular centrosome scaffold in vitro.

Woodruff JB, Wueseke O, Viscardi V, Mahamid J, Ochoa SD, Bunkenborg J, Widlund PO, Pozniakovsky A, Zanin E, Bahmanyar S, Zinke A, Hong SH, Decker M, Baumeister W, Andersen JS, Oegema K, Hyman AA 2015 May Science 6236 348 808-12

All Publications

Soluble tubulin is significantly enriched at mitotic centrosomes.

Baumgart J, Kirchner M, Redemann S, Bond A, Woodruff J, Verbavatz JM, Jülicher F, Müller-Reichert T, Hyman AA, Brugués J, 2019 Dec J. Cell Biol. 12 218 3977-3985

FlexiBAC: a versatile, open-source baculovirus vector system for protein expression, secretion, and proteolytic processing.

Lemaitre RP, Bogdanova A, Borgonovo B, Woodruff JB, Drechsel DN, 2019 03 BMC Biotechnol. 1 19 20

Assembly of Mitotic Structures through Phase Separation.

Woodruff JB 2018 May J. Mol. Biol.

Polo-like kinase phosphorylation determines Caenorhabditis elegans centrosome size and density by biasing SPD-5 toward an assembly-competent conformation.

Wueseke O, Zwicker D, Schwager A, Wong YL, Oegema K, Jülicher F, Hyman AA, Woodruff JB 2016 Oct Biol Open 10 5 1431-1440

Method: In vitro analysis of pericentriolar material assembly.

Woodruff JB, Hyman AA 2015 Methods Cell Biol. 129 369-82

Pericentriolar material structure and dynamics.

Woodruff JB, Wueseke O, Hyman AA 2014 Sep Philos. Trans. R. Soc. Lond., B, Biol. Sci. 1650 369

The Caenorhabditis elegans pericentriolar material components SPD-2 and SPD-5 are monomeric in the cytoplasm before incorporation into the PCM matrix.

Wueseke O, Bunkenborg J, Hein MY, Zinke A, Viscardi V, Woodruff JB, Oegema K, Mann M, Andersen JS, Hyman AA 2014 Oct Mol. Biol. Cell 19 25 2984-92