Sorting nexin 21 is a novel membrane‐binding endonuclease
- Resource Type
- Authors
- Hyun-Jin Kim; Shan Tao; Wonhwa Cho; Seohyeon Song
- Source
- The FASEB Journal. 29
- Subject
- biology
Endosome
Chemistry
Sorting Nexins
Cleavage (embryo)
Biochemistry
Homology (biology)
Cell biology
Sorting nexin
Endonuclease
Genetics
biology.protein
A-DNA
Cell activation
Molecular Biology
Biotechnology
- Language
- ISSN
- 1530-6860
0892-6638
Sorting nexin 21 (SNX21) is a cytosolic protein that contains phox homology (PX) domain. It is localized to early endosomes in a phosphatidylinositol-3-phosphate (PtdIns3P)-dependent manner. Unlike other sorting nexins, SNX21 undergoes autolytic cleavage of the N-terminal region upon cell activation and the truncated SNX21 translocates to nucleus where it function as a DNA endonuclease. To understand the structural basis of these unique functional properties of SNX21, we determined the crystal structures of full-length and N-terminal truncated SNX21. These structures provide an important clue to its cellular function and regulation. Collectively, our work suggests that SNX21 is a new class of novel lipid-dependent endonuclease that may supplement or supplant caspase-activated endonucleases under certain physiological conditions.