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  Cofilin recruits F-actin to SPCA1 and promotes Ca2+-mediated secretory cargo sorting

Kienzle, C., Basnet, N., Crevenna, A. H., Beck, G., Habermann, B., Mizuno, N., et al. (2014). Cofilin recruits F-actin to SPCA1 and promotes Ca2+-mediated secretory cargo sorting. JOURNAL OF CELL BIOLOGY, 206(5), 635-654. doi:10.1083/jcb.201311052.

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 Creators:
Kienzle, Christine1, Author              
Basnet, Nirakar2, Author              
Crevenna, Alvaro H.3, Author
Beck, Gisela4, Author              
Habermann, Bianca5, Author              
Mizuno, Naoko6, Author              
von Blume, Julia1, Author              
Affiliations:
1von Blume, Julia / Molecular Basis of Protein Trafficking, Max Planck Institute of Biochemistry, Max Planck Society, ou_1565173              
2Conti, Elena / Structural Cell Biology, Max Planck Institute of Biochemistry, Max Planck Society, ou_1565144              
3external, ou_persistent22              
4Wedlich-Söldner, Roland / Cellular Dynamics and Cell Patterning, Max Planck Institute of Biochemistry, Max Planck Society, ou_1565174              
5Habermann, Bianca / Computational Biology, Max Planck Institute of Biochemistry, Max Planck Society, ou_1832284              
6Mizuno, Naoko / Cellular and Membrane Trafficking, Max Planck Institute of Biochemistry, Max Planck Society, ou_1688137              

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Free keywords: TRANS-GOLGI NETWORK; PLASMA-MEMBRANE; EPITHELIAL-CELLS; CATHEPSIN-D; LIM-KINASE; COMPLEX; PROTEINS; CALCIUM; ATPASE; APPARATUS
 Abstract: The actin filament severing protein cofilin-1 (CFL-1) is required for actin and P-type ATPase secretory pathway calcium ATPase (SPCA)-dependent sorting of secretory proteins at the trans-Golgi network (TGN). How these proteins interact and activate the pump to facilitate cargo sorting, however, is not known. We used purified proteins to assess interaction of the cytoplasmic domains of SPCA] with actin and CFL-1. A 132-amino acid portion of the SPCA1 phosphorylation domain (P-domain) interacted with actin in a CFL-1-dependent manner. This domain, coupled to nickel nitrilotriacetic acid (Ni-NTA) agarose beads, specifically recruited F-actin in the presence of CFL-1 and, when expressed in He La cells, inhibited Ca2+ entry into the TGN and secretory cargo sorting. Mutagenesis of four amino acids in SPCA1 that represent the CFL-1 binding site also affected Ca2+ import into the TGN and secretory cargo sorting. Altogether, our findings reveal the mechanism of CFL-1-dependent recruitment of actin to SPCA1 and the significance of this interaction for Ca2+ influx and secretory cargo sorting.

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Language(s): eng - English
 Dates: 2014
 Publication Status: Published in print
 Pages: 20
 Publishing info: -
 Table of Contents: -
 Rev. Type: Peer
 Identifiers: ISI: 000341339400008
DOI: 10.1083/jcb.201311052
 Degree: -

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Title: JOURNAL OF CELL BIOLOGY
Source Genre: Journal
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Publ. Info: 1114 FIRST AVE, 4TH FL, NEW YORK, NY 10021 USA : ROCKEFELLER UNIV PRESS
Pages: - Volume / Issue: 206 (5) Sequence Number: - Start / End Page: 635 - 654 Identifier: ISSN: 0021-9525