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Cells
Volume 8
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10.3390/cells8070684
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Article

HIPK2 Phosphorylates the Microtubule-Severing Enzyme Spastin at S268 for Abscission

by
Alessandra Pisciottani
1,†,‡,
Loredana Biancolillo
1,†,
Manuela Ferrara
1,
Davide Valente
2,
Francesca Sardina
1,
Laura Monteonofrio
2,§,
Serena Camerini
3,
Marco Crescenzi
3,
Silvia Soddu
2 and
Cinzia Rinaldo
1,2,*
1
Institute of Molecular Biology and Pathology (IBPM), National Research Council (CNR), c/o Sapienza University, 00185 Rome, Italy
2
Unit of Cellular Networks and Molecular Therapeutic Targets; IRCCS-Regina Elena National Cancer Institute, 00144 Rome, Italy
3
Core Facilities, Italian National Institute of Health, 00161 Rome, Italy
*
Author to whom correspondence should be addressed.
†
These Authors contributed equally to the work.
‡
Present address: Vita-Salute San Raffaele University, 20132, Milan, Italy.
§
Present address: Laboratory of Cardiovascular Science, NIA/NIH Baltimore, MD 21224, USA.
Cells 2019, 8(7), 684; https://doi.org/10.3390/cells8070684
Received: 30 May 2019 / Revised: 2 July 2019 / Accepted: 3 July 2019 / Published: 5 July 2019
(This article belongs to the Special Issue Molecular Factors and Mechanisms Involved in Cytokinesis)
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Abstract

Abscission is the final step of cell division, mediating the physical separation of the two daughter cells. A key player in this process is the microtubule-severing enzyme spastin that localizes at the midbody where its activity is crucial to cut microtubules and culminate the cytokinesis. Recently, we demonstrated that HIPK2, a multifunctional kinase involved in several cellular pathways, contributes to abscission and prevents tetraploidization. Here, we show that HIPK2 binds and phosphorylates spastin at serine 268. During cytokinesis, the midbody-localized spastin is phosphorylated at S268 in HIPK2-proficient cells. In contrast, no spastin is detectable at the midbody in HIPK2-depleted cells. The non-phosphorylatable spastin-S268A mutant does not localize at the midbody and cannot rescue HIPK2-depleted cells from abscission defects. In contrast, the phosphomimetic spastin-S268D mutant localizes at the midbody and restores successful abscission in the HIPK2-depleted cells. These results show that spastin is a novel target of HIPK2 and that HIPK2-mediated phosphorylation of spastin contributes to its midbody localization for successful abscission. View Full-Text
Keywords: HIPK2; spastin; abscission; midbody; phosphorylation HIPK2; spastin; abscission; midbody; phosphorylation
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MDPI and ACS Style

Pisciottani, A.; Biancolillo, L.; Ferrara, M.; Valente, D.; Sardina, F.; Monteonofrio, L.; Camerini, S.; Crescenzi, M.; Soddu, S.; Rinaldo, C. HIPK2 Phosphorylates the Microtubule-Severing Enzyme Spastin at S268 for Abscission. Cells 2019, 8, 684. https://doi.org/10.3390/cells8070684

AMA Style

Pisciottani A, Biancolillo L, Ferrara M, Valente D, Sardina F, Monteonofrio L, Camerini S, Crescenzi M, Soddu S, Rinaldo C. HIPK2 Phosphorylates the Microtubule-Severing Enzyme Spastin at S268 for Abscission. Cells. 2019; 8(7):684. https://doi.org/10.3390/cells8070684

Chicago/Turabian Style

Pisciottani, Alessandra, Loredana Biancolillo, Manuela Ferrara, Davide Valente, Francesca Sardina, Laura Monteonofrio, Serena Camerini, Marco Crescenzi, Silvia Soddu, and Cinzia Rinaldo. 2019. "HIPK2 Phosphorylates the Microtubule-Severing Enzyme Spastin at S268 for Abscission" Cells 8, no. 7: 684. https://doi.org/10.3390/cells8070684

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