Identification of specific lysines and arginines that mediate angiomotin membrane association

Le'Celia Hall, Emily Donovan, Michael Araya, Eniola Idowa, Ilse Jiminez-Segovia, Anthony Folck, Clark Wells, Ann C. Kimble-Hill

Research output: Contribution to journalArticle

Abstract

The family of Angiomotin (Amot) proteins regulate several biological pathways associated with cellular differentiation, proliferation, and migration. These adaptor proteins target proteins to the apical membrane, actin fibers, or the nucleus. A major function of the Amot coiled-coil homology (ACCH) domain is to initiate protein interactions with the cellular membrane, particularly those containing phosphatidylinositol lipids. The work presented in this article uses several ACCH domain lysine/arginine mutants to probe the relative importance of individual residues for lipid binding. This identified four lysine and three arginine residues that mediate full lipid binding. Based on these findings, three of these residues were mutated to glutamates in the Angiomotin 80 kDa splice form and were incorporated into human mammary cell lines. Results show that mutating three of these residues in the context of full-length Angiomotin reduced the residence of the protein at the apical membrane. These findings provide new insight into how the ACCH domain mediates lipid binding to enable Amot proteins to control epithelial cell growth.

Original languageEnglish (US)
Pages (from-to)6726-6736
Number of pages11
JournalACS Omega
Volume4
Issue number4
DOIs
StatePublished - Apr 12 2019

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Arginine
Lysine
Proteins
Membranes
Lipids
Glutamates
Cell growth
Phosphatidylinositols
Actins
Cells
Fibers

ASJC Scopus subject areas

  • Chemistry(all)
  • Chemical Engineering(all)

Cite this

Hall, LC., Donovan, E., Araya, M., Idowa, E., Jiminez-Segovia, I., Folck, A., ... Kimble-Hill, A. C. (2019). Identification of specific lysines and arginines that mediate angiomotin membrane association. ACS Omega, 4(4), 6726-6736. https://doi.org/10.1021/acsomega.9b00165

Identification of specific lysines and arginines that mediate angiomotin membrane association. / Hall, Le'Celia; Donovan, Emily; Araya, Michael; Idowa, Eniola; Jiminez-Segovia, Ilse; Folck, Anthony; Wells, Clark; Kimble-Hill, Ann C.

In: ACS Omega, Vol. 4, No. 4, 12.04.2019, p. 6726-6736.

Research output: Contribution to journalArticle

Hall, LC, Donovan, E, Araya, M, Idowa, E, Jiminez-Segovia, I, Folck, A, Wells, C & Kimble-Hill, AC 2019, 'Identification of specific lysines and arginines that mediate angiomotin membrane association', ACS Omega, vol. 4, no. 4, pp. 6726-6736. https://doi.org/10.1021/acsomega.9b00165
Hall LC, Donovan E, Araya M, Idowa E, Jiminez-Segovia I, Folck A et al. Identification of specific lysines and arginines that mediate angiomotin membrane association. ACS Omega. 2019 Apr 12;4(4):6726-6736. https://doi.org/10.1021/acsomega.9b00165
Hall, Le'Celia ; Donovan, Emily ; Araya, Michael ; Idowa, Eniola ; Jiminez-Segovia, Ilse ; Folck, Anthony ; Wells, Clark ; Kimble-Hill, Ann C. / Identification of specific lysines and arginines that mediate angiomotin membrane association. In: ACS Omega. 2019 ; Vol. 4, No. 4. pp. 6726-6736.
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