Figure S1.
Predicted isoforms and motor-binding domains of Nesprin-2. (A) The relative abundance of Nesprin-2 transcripts was analyzed by MISO. Both Syne2-210 and Syne2-201 are translated as the full-length Nesprin-2G. Syne2-206 undergoes nonsense-mediated decay. (B) Sequence alignment of the putative Spindly motifs (left) and CC1 box motifs (right) of Nesprin-2 and other dynein adaptors. Asterisks indicate conserved amino acids. Adapted from Olenick and Holzbaur (2019). (C) Predicted protein structure of SR52-KASH and SR48-KASH by ColabFold. Different colors correspond to different SRs. Black arrows indicate the LEWD motif, green arrows indicate the putative Spindly motifs, and red arrows indicate the putative CC1 motifs. Related to Video 2. (D) The putative coiled-coil domains of SR48-KASH were predicted by Deepcoil2.

Predicted isoforms and motor-binding domains of Nesprin-2. (A) The relative abundance of Nesprin-2 transcripts was analyzed by MISO. Both Syne2-210 and Syne2-201 are translated as the full-length Nesprin-2G. Syne2-206 undergoes nonsense-mediated decay. (B) Sequence alignment of the putative Spindly motifs (left) and CC1 box motifs (right) of Nesprin-2 and other dynein adaptors. Asterisks indicate conserved amino acids. Adapted from Olenick and Holzbaur (2019). (C) Predicted protein structure of SR52-KASH and SR48-KASH by ColabFold. Different colors correspond to different SRs. Black arrows indicate the LEWD motif, green arrows indicate the putative Spindly motifs, and red arrows indicate the putative CC1 motifs. Related to Video 2. (D) The putative coiled-coil domains of SR48-KASH were predicted by Deepcoil2.

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