ADAM22 plays an important role in cell adhesion and spreading with the assistance of 14-3-3

Zhu, Pengcheng; Sang, Yingying; Xu, Huanbing; Zhao, Jing; Xu, Rener; Sun, Yubo; Xu, Tianhong; Wang, Xiaolei; Chen, Linfeng; Feng, Hanping; Li, Changben; Zhao, Shouyuan

doi:10.1016/j.bbrc.2005.03.229

Cited by 23 publications

(19 citation statements)

References 40 publications

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“…During the course of our studies, reports of ADAM22 interacting with some 14-3-3 proteins were published (Zhu et al, 2005;Zhu et al, 2003). Here, we report the interaction of ADAM22 with all 14-3-3 protein family members expressed in the brain and suggest a novel function for these interactions, where 14-3-3 binding may play a role in the forward transport of ADAM22 to the cell membrane.…”

Section: Introductionmentioning

confidence: 66%

Efficient ADAM22 surface expression is mediated by phosphorylation-dependent interaction with 14-3-3 protein family members

Gödde

D'Abaco

Paradiso

et al. 2006

Journal of Cell Science

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ADAM22 is one of three catalytically inactive ADAM family members highly expressed in the brain. ADAM22 has numerous splice variants, all with considerable cytoplasmic tails of up to 148 amino acids. ADAM22 can act to inhibit cell proliferation, however, it has been suggested that it also acts as an adhesion protein. We identified three 14-3-3 protein members by a yeast twohybrid screen and show by co-immunoprecipitation that the cytoplasmic domain of ADAM22 can interact with all six 14-3-3 proteins expressed in the brain. In addition, we show that 14-3-3 proteins interact preferentially with the serine phosphorylated precursor form of ADAM22. ADAM22 has two 14-3-3 protein binding consensus motifs; the first binding site, spanning residues 831-834, was shown to be the most crucial for 14-3-3 binding to occur. The interaction between ADAM22 and 14-3-3 proteins is dependent on phosphorylation of ADAM22, but not of 14-3-3 proteins. ADAM22 point mutants lacking functional 14-3-3 protein binding motifs could no longer accumulate efficiently at the cell surface. Deletion of both 14-3-3 binding sites and newly identified ER retention motifs restored localization of ADAM22 at the cell surface. These results reveal a role for 14-3-3 proteins in targeting ADAM22 to the membrane by masking ER retention signals.

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Section: Introductionmentioning

confidence: 66%

Efficient ADAM22 surface expression is mediated by phosphorylation-dependent interaction with 14-3-3 protein family members

Gödde

D'Abaco

Paradiso

et al. 2006

Journal of Cell Science

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“…The enhanced ability gained by exogenous ADAM22 and 14-3-3zeta is much more than the summation of enhancement effect of ADAM22 and 14-3-3zeta individually. 57,58 The interaction between 14-3-3zeta and ADAM22 affects cell adhesion and spreading. The overexpression of exogenous ADAM22 with 14-3-3zeta-binding motifs in HEK293 cells could significantly enhance cell adhesion and spreading, compared with the truncated ADAM22 lack of 14-3-3-binding motifs.…”

Section: Cell Skeleton Invasion and Metastasismentioning

confidence: 99%

“…The overexpression of exogenous ADAM22 with 14-3-3zeta-binding motifs in HEK293 cells could significantly enhance cell adhesion and spreading, compared with the truncated ADAM22 lack of 14-3-3-binding motifs. 57 14-3-3zeta in cancer X Yang et al…”

Section: Cell Skeleton Invasion and Metastasismentioning

confidence: 99%

Targeting 14-3-3zeta in cancer therapy

et al. 2011

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“…In addition, ADAM22 is a receptor for leucine-rich glioma inactivated 1 (LGI1), which regulates synaptic transmission in cells [60]. The cytoplasmic domain of ADAM22 interacts with 14-3-3ζ protein, which is required for cell adherence and cell spreading [61]. Our results show that ADAM22 is expressed in high amounts in the chicken brain from about E12 to E20 (Fig.…”

Section: Adam22mentioning

confidence: 68%

Quantitative and dynamic expression profile of premature and active forms of the regional ADAM proteins during chicken brain development

Markus

Yan

Rolfs

et al. 2011

Cellular and Molecular Biology Letters

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Abstract:The ADAM (A Disintegrin and Metalloprotease) family of transmembrane proteins plays important roles in embryogenesis and tissue formation based on their multiple functional domains. In the present study, for the first time, the expression patterns of the premature and the active forms of six members of the ADAM proteins -ADAM9, ADAM10, ADAM12, ADAM17, ADAM22 and ADAM23 -in distinct parts of the developing chicken brain were investigated by quantitative Western blot analysis from embryonic incubation day (E) 10 to E20. The results show that the premature and the active forms of various ADAM proteins are spatiotemporally regulated in different parts of the brain during development, suggesting that the ADAMs play a very important role during embryonic development.

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ADAM22 plays an important role in cell adhesion and spreading with the assistance of 14-3-3

Cited by 23 publications

References 40 publications

Efficient ADAM22 surface expression is mediated by phosphorylation-dependent interaction with 14-3-3 protein family members

Efficient ADAM22 surface expression is mediated by phosphorylation-dependent interaction with 14-3-3 protein family members

Targeting 14-3-3zeta in cancer therapy

Quantitative and dynamic expression profile of premature and active forms of the regional ADAM proteins during chicken brain development

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