Immuno-electron microscopy localizes Caenorhabditis elegans vitellogenins along the classic exocytosis route

Author:

Zhai Chao123ORCID,Zhang Nan14ORCID,Li Xi-Xia5ORCID,Tan Xue-Ke5,Sun Fei567ORCID,Dong Meng-Qiu14ORCID

Affiliation:

1. National Institute of Biological Sciences , Beijing 102206 , China

2. School of Life Sciences, Peking University , Beijing 100871 , China

3. Tsinghua University Tsinghua Institute of Multidisciplinary Biomedical Research, , Beijing 100084 , China

4. Tsinghua Institute of Multidisciplinary Biomedical Research, Tsinghua University , Beijing 100084 , China

5. Center for Biological Imaging, Institute of Biophysics, Chinese Academy of Sciences , Beijing 100101 , China

6. National Key Laboratory of Biomacromolecules, CAS Center for Excellence in Biomacromolecules, Institute of Biophysics, Chinese Academy of Sciences , Beijing 100101 , China

7. University of Chinese Academy of Sciences , School of Life Science, Beijing 100049 , China

Abstract

Abstract Vitellogenins (VITs) are the most abundant proteins in adult hermaphrodite Caenorhabditis elegans. VITs are synthesized in the intestine, secreted to the pseudocoelom, matured into yolk proteins, and finally deposited in oocytes as nutrients for progeny development. How VITs are secreted out of the intestine remains unclear. Using immuno-electron microscopy (immuno-EM), we localize intestinal VITs along an exocytic pathway consisting of the rough endoplasmic reticulum (ER), the Golgi, and the lipid bilayer-bounded VIT vesicles (VVs). This suggests that the classic exocytotic pathway mediates the secretion of VITs from the intestine to the pseudocoelom. We also show that pseudocoelomic yolk patches (PYPs) are membrane-less and amorphous. The different VITs/yolk proteins are packed as a mixture into the above structures. The size of VVs can vary with the VIT levels and the age of the worm. On adult Day 2 (AD 2), intestinal VVs (~200 nm in diameter) are smaller than gonadal yolk organelles (YOs, ~500 nm in diameter). VVs, PYPs, and YOs share a uniform medium electron density by conventional EM. The morphological profiles documented in this study serve as a reference for future studies of VITs/yolk proteins.

Funder

National Natural Science Foundation of China

Ministry of Science and Technology

People's Republic of China

National High-Level Talents Special Support Program

Beijing Municipal Science and Technology Commission

Publisher

Oxford University Press (OUP)

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