Cell Division Mechanisms


About the group:

Cytoplasmic dynein 1 (dynein), a mega-dalton complex of 6 distinct subunits, is the predominant microtubule minus end-directed motor in animals and participates in a wide range of essential cellular activities, ranging from the transport of proteins, mRNA, and vesicles to nuclear migration and cell division. Our group is interested in the regulatory mechanisms that give rise to dynein's functional diversity.

Image: Immunofluorescence image of the first mitotic division in the C. elegans embryo: microtubule-based motor proteins like cytoplasmic dynein participate in the assembly of the mitotic spindle (green) and the segregation of chromosomes (purple).



We use live-cell fluorescence microscopy, genetics, and biochemical approaches in the roundworm Caenorhabditis elegans and human cultured cells to study the roles and molecular mechanisms of co-factors that associate with dynein to modulate localization, interaction with cargo, and motor activity. We have been investigating how the 3-subunit Rod-Zw10-Zwilch complex and the adaptor protein Spindly regulate dynein function at the kinetochore, the site on chromosomes where spindle microtubules attach to drive the segregation of sister chromatids during cell division. Adaptors like Spindly have a dual role: they bring dynein together with its essential processivity factor dynactin, which is itself a multi-subunit complex, and they establish the link to diverse cargo. By studying how different adaptor families interact with dynein and dynactin, we hope to uncover general and cargo-specific mechanisms underlying the assembly and activation of the dynein-dynactin transport machinery in dividing and non-dividing cells. Mutations in dynein and its regulators are known to cause neurodegenerative disease, making a molecular understanding of dynein-driven transport medically relevant.


Selected Publications:

For all publications from R. Gassmann click here.

Barbosa D.J., Duro J., Prevo B., Cheerambathur D.K., Carvalho A.X., Gassmann R. (2017) Dynactin binding to tyrosinated microtubules promotes centrosome centration in C. elegans by enhancing dynein-mediated organelle transport. PLOS Genet. 13: e1006941.

Gama J.B., Pereira C., Simões P.A., Celestino R., Reis R.M., Barbosa D.J., Pires H.R., Carvalho C., Amorim J., Carvalho A.X., Cheerambathur D.K., Gassmann R. (2017) Molecular mechanism of dynein recruitment to kinetochores by the Rod/Zw10/Zwilch complex and Spindly. J. Cell Biol. 216: 943-960.

Andrew A.J., Reis R.M., Niessen S., Pereira C., Andres D.A., Spielmann H.P., Cleveland D.W., Desai A., Gassmann R. (2015) Preventing farnesylation of the dynein adaptor Spindly contributes to the mitotic defects caused by farnesyltransferase inhibitors. Mol. Biol. Cell 26: 1845-1856.

Cheerambathur D.K., Gassmann R., Cook B., Oegema K., Desai A. (2013) Crosstalk between microtubule attachment complexes ensures accurate chromosome segregation. Science 342: 1239-42.

Gassmann R., Rechtsteiner A., Yuen K.W., Muroyama A., Barron F., Maddox P., Monen J., Egelhofer T., Ercan S., Oegema K., Lieb J., Strome S., Desai A. (2012) An inverse relationship to germline transcription defines centromeric chromatin in C. elegans. Nature 484: 534-7.

Gassmann R., Holland A.J., Varma D., Wan X., Çivril F., Cleveland D.W., Oegema K., Salmon E.D., Desai A. (2010) Removal of Spindly from microtubule-attached kinetochores controls spindle checkpoint silencing in human cells. Genes Dev. 24:957-71.

Gassmann R., Essex A., Hu J.S., Maddox P.S., Motegi F., Sugimoto A., O'Rourke S.M., Bowerman B., McLeod I., Yates J.R. 3rd, Oegema K., Cheeseman I.M., Desai A. (2008) A new mechanism controlling kinetochore-microtubule interactions revealed by comparison of two dynein-targeting components: SPDL-1 and the Rod/Zwilch/Zw10 complex. Genes Dev. 22:2385-99.

Group Leader

Abreu, Carla Manuela

Celestino, Ricardo

Dantas, Tiago

José Barbosa, Daniel

Rodrigues, Artur Filipe


Gama, José Bernardo

Magalhães e Silva, Tânia

Phd Students

Carvalho Simões, Patrícia

Rocha, Helder

MSc Students

Vieira, Cármen


Carvalho, Cátia

Ferreira, Vanessa

Teixeira, Vanessa

Walsh, Grace


Castro, Ana Rita

Kačenauskaitė, Lina

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