2025/04/28
paper · doi:10.17912/micropub.biology.001595
<p><i>Schizosaccharomyces pombe</i> <a href="https://www.pombase.org/spombe/result/SPBC428.13c" id="8ab091fb-c53e-40bc-a76a-4b4ede63d65f">Mob1</a> is the regulatory subunit of the protein kinase <a href="https://www.pombase.org/spombe/result/SPAC24B11.11c" id="50b81920-44f5-4450-aa42-164646b6407b">Sid2</a>. The Sid2-<a href="https://www.pombase.org/spombe/result/SPBC428.13c" id="b0019f45-d894-464e-82a7-258102688e8f">Mob1</a> complex is the most downstream acting component of the septation initiation network (SIN). In the absence of functional <a href="https://www.pombase.org/spombe/result/SPBC428.13c" id="c70cd3f8-f2a5-4eac-8be1-c61d65b09c05">Mob1</a>, cells fail cytokinesis and become multinucleate. Here we characterize a set of temperature-sensitive <i><a href="https://www.pombase.org/spombe/result/SPBC428.13c" id="d120a280-e391-43f6-afaa-1315d9e98bda">mob1</a> </i>alleles by identifying the mutations within each allele, characterizing the extent of their growth defects, and visualizing the cell defects. Based on structural modeling, we hypothesize that the <a href="https://www.pombase.org/spombe/result/SPBC428.13c" id="e6e96237-0e57-4fe5-bd47-57d0bf6465d4">Mob1</a> mutations interfere with <a href="https://www.pombase.org/spombe/result/SPBC428.13c" id="040c8632-abea-42ca-8804-541a2dc1f7e3">Mob1</a> stability and its ability to bind the N-terminal regulatory region of <a href="https://www.pombase.org/spombe/result/SPAC24B11.11c" id="4bff760e-c127-496a-9def-f930c9696a09">Sid2</a>.</p>