Journal article
Cellular uptake of the Antennapedia homeodomain polypeptide by macropinocytosis.
- 2013-12-24
Published in:
- Biochemical and biophysical research communications. - 2014
Antennapedia homeodomain
Cell-Penetrating Peptides (CPPs)
Penetratin
Amino Acid Sequence
Antennapedia Homeodomain Protein
HEK293 Cells
HeLa Cells
Homeodomain Proteins
Humans
Models, Molecular
Molecular Sequence Data
Peptide Fragments
Pinocytosis
Protein Structure, Tertiary
Recombinant Proteins
English
Antennapedia homeodomain has been shown to be able to translocate from extracellular space into the cytoplasm of cells in a receptor-independent manner. Its third α-helix domain, designated as "Penetratin", was proposed to be the functional transduction domain that is responsible for the translocation, and it is widely used for intracellular delivery of various exogenous proteins. Although Penetratin has been regarded to be the only element conferring the capacity on its parent polypeptide to penetrate through the plasma membrane, we found that the complete Antennapedia homeodomain exhibits an appreciably higher level of translocation efficiency as compared to Penetratin. Pharmacological analysis demonstrated that macropinocytic endocytosis plays a significant role underlying the process of the homeodomain internalization, and this is consistent with the observation that internalized polypeptide co-localizes with a fluid phase dye. Our results identify macropinocytosis as a major mechanism by which Antennapedia homeodomain obtains the access to the interior of cells, providing a novel perspective in the field of protein translocation and transduction.
- Language
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- English
- Open access status
- hybrid
- Identifiers
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- DOI 10.1016/j.bbrc.2013.12.062
- PMID 24361959
- Persistent URL
- https://folia.unifr.ch/global/documents/53508
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