Structural characterization of coatomer in its cytosolic state.
10.1007/s13238-016-0296-z
- Author:
Shengliu WANG
1
;
Yujia ZHAI
1
;
Xiaoyun PANG
1
;
Tongxin NIU
1
;
Yue-He DING
2
;
Meng-Qiu DONG
2
;
Victor W HSU
3
;
Zhe SUN
4
;
Fei SUN
5
Author Information
1. National Key Laboratory of Biomacromolecules, Institute of Biophysics, Chinese Academy of Sciences, Beijing, 100101, China.
2. National Institute of Biological Sciences, Beijing, Beijing, 102206, China.
3. Department of Medicine, Harvard Medical School, Brigham and Women's Hospital, Boston, MA, 02115, USA.
4. National Key Laboratory of Biomacromolecules, Institute of Biophysics, Chinese Academy of Sciences, Beijing, 100101, China. zsun@moon.ibp.ac.cn.
5. National Key Laboratory of Biomacromolecules, Institute of Biophysics, Chinese Academy of Sciences, Beijing, 100101, China. feisun@ibp.ac.cn.
- Publication Type:Journal Article
- Keywords:
COPI;
coatomer;
human;
membrane trafficking;
single-particle electron microscopy
- MeSH:
ADP-Ribosylation Factor 1;
chemistry;
metabolism;
Animals;
Coatomer Protein;
chemistry;
metabolism;
Cytosol;
chemistry;
metabolism;
GTPase-Activating Proteins;
chemistry;
metabolism;
Humans;
Membranes, Artificial;
Rats
- From:
Protein & Cell
2016;7(8):586-600
- CountryChina
- Language:English
-
Abstract:
Studies on coat protein I (COPI) have contributed to a basic understanding of how coat proteins generate vesicles to initiate intracellular transport. The core component of the COPI complex is coatomer, which is a multimeric complex that needs to be recruited from the cytosol to membrane in order to function in membrane bending and cargo sorting. Previous structural studies on the clathrin adaptors have found that membrane recruitment induces a large conformational change in promoting their role in cargo sorting. Here, pursuing negative-stain electron microscopy coupled with single-particle analyses, and also performing CXMS (chemical cross-linking coupled with mass spectrometry) for validation, we have reconstructed the structure of coatomer in its soluble form. When compared to the previously elucidated structure of coatomer in its membrane-bound form we do not observe a large conformational change. Thus, the result uncovers a key difference between how COPI versus clathrin coats are regulated by membrane recruitment.
