Proteomics

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Quantitative Proteomics Illuminates A Functional Interaction Between Mouse Homolog Of Diaphanous 2 (mDia2) And The Proteasome

ABSTRACT: Formin mDia2 is a cytoskeleton-regulatory protein that switches reversibly between a closed, auto-inhibited and an open, active conformation. Although the open conformation of mDia2 induces actin assembly thereby controlling many cellular processes, mDia2 possesses also actin-independent and conformation-insensitive scaffolding roles related to microtubules and p53, respectively. Thus, we hypothesise that mDia2 may have other unappreciated functions and regulatory modes. Here we identify and validate proteasome and Ubiquitin as genuine mDia2-interacting partners using quantitative proteomics and a multi-disciplinary approach, respectively.

INSTRUMENT(S): LTQ Orbitrap

ORGANISM(S): Homo Sapiens (human)

TISSUE(S): Epithelial Cell, Hela Cell

SUBMITTER: Onno Bleijerveld  

LAB HEAD: A.F. Maarten Altelaar

PROVIDER: PXD002066 | Pride | 2016-12-14

REPOSITORIES: Pride

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MaxQuant_OutputSample_IDs_mDia2_IPs_SILAC.zip Other
OR3_110601_SSG_NKI_Robgel2_2A1.raw Raw
OR3_110601_SSG_NKI_Robgel2_2A10.raw Raw
OR3_110601_SSG_NKI_Robgel2_2A2.raw Raw
OR3_110601_SSG_NKI_Robgel2_2A3.raw Raw
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Quantitative Proteomics Illuminates a Functional Interaction between mDia2 and the Proteasome.

Isogai Tadamoto T   van der Kammen Rob R   Bleijerveld Onno B OB   Goerdayal Soenita S SS   Argenzio Elisabetta E   Altelaar A F Maarten AF   Innocenti Metello M  

Journal of proteome research 20161107 12

Formin mDia2 is a cytoskeleton-regulatory protein that switches reversibly between a closed, autoinhibited and an open, active conformation. Although the open conformation of mDia2 induces actin assembly thereby controlling many cellular processes, mDia2 possesses also actin-independent and conformation-insensitive scaffolding roles related to microtubules and p53, respectively. Thus, we hypothesize that mDia2 may have other unappreciated functions and regulatory modes. Here we identify and vali  ...[more]

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