8waf
From Proteopedia
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== Function == | == Function == | ||
[https://www.uniprot.org/uniprot/CHUP1_ARATH CHUP1_ARATH] Required for the positioning and movement of chloroplasts. Interacts with profilin and actin independent of its polymerization status. Regulates chloroplast localization by anchoring chloroplasts to the plasma membrane and forming a bridge to the actin cytoskeleton.<ref>PMID:12490952</ref> <ref>PMID:14615600</ref> <ref>PMID:18193273</ref> <ref>PMID:18715957</ref> | [https://www.uniprot.org/uniprot/CHUP1_ARATH CHUP1_ARATH] Required for the positioning and movement of chloroplasts. Interacts with profilin and actin independent of its polymerization status. Regulates chloroplast localization by anchoring chloroplasts to the plasma membrane and forming a bridge to the actin cytoskeleton.<ref>PMID:12490952</ref> <ref>PMID:14615600</ref> <ref>PMID:18193273</ref> <ref>PMID:18715957</ref> | ||
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| - | == Publication Abstract from PubMed == | ||
| - | Plants have unique responses to fluctuating light conditions. One such response involves chloroplast photorelocation movement, which optimizes photosynthesis under weak light by the accumulation of chloroplasts along the periclinal side of the cell, which prevents photodamage under strong light by avoiding chloroplast positioning toward the anticlinal side of the cell. This light-responsive chloroplast movement relies on the reorganization of chloroplast actin (cp-actin) filaments. Previous studies have suggested that CHLOROPLAST UNUSUAL POSITIONING 1 (CHUP1) is essential for chloroplast photorelocation movement as a regulator of cp-actin filaments. In this study, we conducted comprehensive analyses to understand CHUP1 function. Functional, fluorescently-tagged CHUP1 colocalized with and was coordinately reorganized with cp-actin filaments on the chloroplast outer envelope during chloroplast movement in Arabidopsis thaliana. CHUP1 distribution was reversibly regulated in a blue light- and phototropin-dependent manner. X-ray crystallography revealed that the CHUP1 C-terminal domain shares structural homology with the formin homology 2 (FH2) domain, despite lacking sequence similarity. Furthermore, the CHUP1 C-terminal domain promoted actin polymerization in the presence of profilin in vitro. Taken together, our findings indicate that CHUP1 is a plant-specific actin polymerization factor that has convergently evolved to assemble cp-actin filaments and enables chloroplast photorelocation movement. | ||
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| - | CHLOROPLAST UNUSUAL POSITIONING 1 is a plant-specific actin polymerization factor regulating chloroplast movement.,Kong SG, Yamazaki Y, Shimada A, T Kijima S, Hirose K, Katoh K, Ahn J, Song HG, Han JW, Higa T, Takano A, Nakamura Y, Suetsugu N, Kohda D, Uyeda TQP, Wada M Plant Cell. 2023 Dec 22:koad320. doi: 10.1093/plcell/koad320. PMID:38134410<ref>PMID:38134410</ref> | ||
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| - | From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br> | ||
| - | </div> | ||
| - | <div class="pdbe-citations 8waf" style="background-color:#fffaf0;"></div> | ||
== References == | == References == | ||
<references/> | <references/> | ||
Current revision
Crystal structure of the C-terminal fragment (residues 756-982 with the C864S mutation) of Arabidopsis thaliana CHUP1
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