(A) Multiple phosphorylation regulates Mps3 localisation and motion in NE during meiosis. In mitotic cells, Mps3 (green) is mainly located in the SPB. In some strain, disperse weak Mps3 signal is detected on NE, which might be regulated by DDK. Upon entry into meiosis, Mps3 forms a few foci on NE in early prophase I, and phosphorylation of the luminal region of Mps3 and, probably DDK, promotes localisation of more Mps3 proteins as focus/patch on NE. Mps3 foci/patches transiently form a cluster of some Mps3 foci by an unknown mechanism, and CDK and DDK and Rec8-cohesin promote dissociation of Mps3 and Rap1(telomere) clusters. It is likely that positive feedback on Mps3 phosphorylation would increase the localisation of Mps3 on NEs, which results in full NE coverage of Mps3. (B) A hypothetical model of the formation of Mps3-containing LINC complex. During mitosis, Mps3 forms a non-canonical LINC complex with cis-membrane interactions with Mps2 as a component of the half-bridge and SPIN (left). Upon induction of meiosis, unknown factors promote the formation of Mps3 foci on NE. Then, the JM region of Mps3 is subject to non-canonical phosphorylation, which might in turn weaken the binding of JM to INM, probably by electric repulsion between the JM regions with negative charges and acid lipids. This process promotes the formation of the canonical LINC complex with the trans-membrane configuration, in which the Mps3 SUN domain binds to the KASH domain of Mps2 and Csm4. Csm4 may promote structural changes in the luminal region of Mps2. The N-terminal region of Mps3, which is located in the nucleoplasm, binds to a telomere-binding protein, Ndj1. During middle and late prophase I, Mps3 forms a large protein ensemble on the NE, which is seen as a patch.