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. 2021 Oct 20;134(20):jcs259134. doi: 10.1242/jcs.259134

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© 2021. Published by The Company of Biologists Ltd

This is an Open Access article distributed under the terms of the Creative Commons Attribution License (https://creativecommons.org/licenses/by/4.0), which permits unrestricted use, distribution and reproduction in any medium provided that the original work is properly attributed.

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Fig. 7. — Overall charge, rather than specific phosphosites modulate RLP44 function. (A) Phosphatase treatment of pRLP44:RLP44-(GS)₁₁-GFP leads to a pronounced shift in electrophoretic mobility, visualized by western blotting using GFP antiserum. (B) The relative abundance of the lower mobility, phosphatase-sensitive RLP44–(GS)11–GFP band is responsive to 24-Epibrassinolide (BL) and kinase inhibitor treatment. (C) The Pdead version of pRLP44:RLP44-(GS)11-GFP is able to complement cnu2 in a similar manner to the WT and Pmimic versions. (D) All three RLP44–(GS)₁₁–GFP versions mainly accumulate at the plasma membrane. Scale bars: 5 µm. Images representative of three experiments. Image width=7.25 cm.