WormBase Tree Display for Picture: WBPicture0000015047

WBPicture0000015047 Description: Figure 1. A missense mutation in UNC-112 eliminates binding to PAT-4 and localization to integrin adhesion complexes in muscle: A. A missense mutation in UNC-112 eliminates specific binding to PAT-4 using the yeast two hybrid system. Numbers indicate amino acid residue numbers in UNC-112. + represents growth on His- plate and Ade- plate. - represents no growth on His- plate and Ade- plate. Wild type UNC-112 can bind to PAT-3 and PAT-4. UNC-112 with E302G cannot bind to PAT-4, but still can bind to PAT-3. B. Western blot of lysates from transgenic worms. Worms carrying HA-tagged UNC-112 E302G, expressed from a heat shock promoter, with heat shock (+) or without heat shock (−), reacted with anti-HA. C. Localization of heat shock-expressed HA-tagged wild type and E302G UNC-112 in transgenic animals. Worms were immunostained with anti-HA to detect the transgenic UNC-112 and with anti-UNC-95 to visualize the optical plane in body wall muscle cells that contain the integrin adhesion complexes (dense bodies and M-lines). Wild type HA-UNC-112 localizes normally to dense bodies and M-lines. However, E302G HA-UNC-112 fails to localize to these structures. White bar, 10 μm. D. Alignment of UNC-112, Kindlin-3, Kindlin-1 and Kindlin-2. Multiple polypeptide sequences were aligned using Clustal Omega (Madeira et al. 2019). E302 is shown in cyan, and D382 is shown in green. E. Structure of UNC-112 based on the human kindlin-3 3D structure (PDB: 7C3M) (Bu et al., 2020) modelled with SWISS-MODEL (Waterhouse et al., 2018), and showing D382 and E302 residues. UNC-112 with the D382V mutation also cannot bind to PAT-4 (Qadota et al. 2012).
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  Acknowledgment: Template: Reprinted from <Journal_URL>
    Publication_year: 2021
    Article_URL: DOI id 10.17912/micropub.biology.000454
    Journal_URL: microPublicationBiology
    Publisher_URL: Micropublication
  Reference: WBPaper00061880