Related Experiment Video
Updated: Jun 8, 2026

Investigating the Function of Coronin A in the Early Starvation Response of Dictyostelium discoideum by Aggregation Assays
Published on: June 18, 2016
SunB, a novel Sad1 and UNC-84 domain-containing protein required for development of Dictyostelium discoideum
Nao Shimada1, Kei Inouye, Satoshi Sawai
1Department of Biology, Faculty of Science, Toho University, 2-2-1 Miyama, Funabashi, Chiba 274-8510, Japan.
Abstract:
A gene, sunB, encoding a novel class of Sad1 and UNC-84 (SUN) domain, was isolated from a cDNA screen for suppressors of a mutation in Dd-STATa - a Dictyostelium homologue of metazoan STAT (signal transducers and activators of transcription). The SunB protein localized in the area around the nucleus in growing cells, but in the multicellular stages it was predominantly found in prespore vacuoles (PSVs). A disruptant of sunB was multinucleated in the vegetative phase; during development it formed mounds with multiple tips and failed to culminate. The mutation was cell autonomous, and showed reduced expression of the prespore marker gene pspA and elevated expression of marker genes for prestalk AB cells. Interestingly, the level of SunB was abnormally high in the prestalk cells of Dd-STATa mutants, which are defective in culmination. We conclude that SunB is essential for accurate prestalk/prespore differentiation during Dictyostelium development and that its cell-type dependent localization is regulated by a Dd-STATa-mediated signaling pathway.
Related Concept Videos
Conservation of Protein Domains Over Different Proteins
A limited set of protein domains often duplicate and recombine during evolution. These domains can be organized in different combinations to form...
Pinching-off of Coated Vesicles
Nucleoid
Overview of Secretory Vesicles
Various proteins regulate the aggregation of molecules inside the secretory vesicles. Chromogranins...
piRNA - Piwi-interacting RNAs
Rab Proteins
Rab proteins switch between a cytosolic, GDP-bound inactive state and a membrane-anchored, GTP-bound active state. By themselves, Rabs show slow rates of GDP/GTP exchange and GTP hydrolysis. Thus, Rab proteins are considered...

