Chromokinesin KIF4A teams up with stathmin 1 to regulate abscission in a SUMO-dependent manner.

Cell division ends when two daughter cells physically separate via abscission, the cleavage of the intercellular bridge. It is not clear how the anti-parallel microtubule bundles bridging daughter cells are severed. Here, we present a novel abscission mechanism.

A comparison of international clinical practice guidelines on adult chronic rhinosinusitis shows considerable variability of recommendations for diagnosis and treatment.

Objectives: To compare international clinical practice guidelines on adult chronic rhinosinusitis (CRS).

Design: Extensive literature search in Embase, PubMed and the internet (Google, websites of well-known guideline organizations) on November 21st 2018.

Main Outcome Measures: Guidelines' quality was measured by the AGREE II instrument.

SUMO targets the APC/C to regulate transition from metaphase to anaphase.

Signal transduction by small ubiquitin-like modifier (SUMO) regulates a myriad of nuclear processes. Here we report on the role of SUMO in mitosis in human cell lines. Knocking down the SUMO conjugation machinery results in a delay in mitosis and defects in mitotic chromosome separation.

Guiding Mitotic Progression by Crosstalk between Post-translational Modifications.

Cell division is tightly regulated to disentangle copied chromosomes in an orderly manner and prevent loss of genome integrity. During mitosis, transcriptional activity is limited and post-translational modifications (PTMs) are responsible for functional protein regulation. Essential mitotic regulators, including polo-like kinase 1 (PLK1) and cyclin-dependent kinases (CDK), as well as the anaphase-promoting complex/cyclosome (APC/C), are members of the enzymatic machinery responsible for protein modification.

Converging Small Ubiquitin-like Modifier (SUMO) and Ubiquitin Signaling: Improved Methodology Identifies Co-modified Target Proteins.

Post-translational protein modifications (PTMs) including small chemical groups and small proteins, belonging to the ubiquitin family, are essential for virtually all cellular processes. In addition to modification by a single PTM, proteins can be modified by a combination of different modifiers, which are able to influence each other. Because little is known about crosstalk among different ubiquitin family members, we developed an improved method enabling identification of co-modified proteins on a system-wide level using mass spectrometry.