Display of membrane proteins on the heterologous caveolae carved by caveolin-1 in the Escherichia coli cytoplasm

Jonghyeok Shin, Young Hun Jung, Da Hyeong Cho, Myungseo Park, Kyung Eun Lee, Yoosoo Yang, Cherlhyun Jeong, Bong Hyun Sung, Jung Hoon Sohn, Jin Byung Park, Dae Hyuk Kweon

Research output: Contribution to journalArticlepeer-review

14 Scopus citations


Caveolae are membrane-budding structures that exist in many vertebrate cells. One of the important functions of caveolae is to form membrane curvature and endocytic vesicles. Recently, it was shown that caveolae-like structures were formed in Escherichia coli through the expression of caveolin-1. This interesting structure seems to be versatile for a variety of biotechnological applications. Targeting of heterologous proteins in the caveolae-like structure should be the first question to be addressed for this purpose. Here we show that membrane proteins co-expressed with caveolin-1 are embedded into the heterologous caveolae (h-caveolae), the cavaolae-like structures formed inside the cell. Two transmembrane SNARE (soluble N-ethylmaleimide-sensitive factor attachment protein receptor) proteins, Syntaxin 1a and vesicle-associated membrane protein 2 (VAMP2), were displayed on the h-caveolae surface. The size of the h-caveolae harboring the transmembrane proteins was ~100. nm in diameter. The proteins were functional and faced outward on the h-caveolae. Multi-spanning transmembrane proteins FtsH and FeoB could be included in the h-caveolae, too. Furthermore, the recombinant E. coli cells were shown to endocytose substrate supplemented in the medium. These results provide a basis for exploiting the h-caveolae formed inside E. coli cells for future biotechnological applications.

Original languageEnglish
Pages (from-to)55-62
Number of pages8
JournalEnzyme and Microbial Technology
StatePublished - 1 Nov 2015

Bibliographical note

Publisher Copyright:
© 2015 Elsevier Inc.


  • Caveolin-1
  • Heterologous caveolae
  • Transmembrane protein


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