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Identification of the cross-linked ELMO1-DOCK5-Rac1 complex.

ABSTRACT: The ELMO1-DOCK5-Rac1 complex is a dimer of heterotrimers centered on a homodimer of the DOCK5 DHR-2 domain. We analyzed the ELMO1-DOCK5-Rac1 complex by cross-linking mass spectrometry and identified intermolecular cross-links between Rac1, ELMO1, and DOCK5.

ORGANISM(S): Homo Sapiens (human)

SUBMITTER: Mikako Shirouzu

PROVIDER: PXD026097 | JPOST Repository | Tue May 25 00:00:00 BST 2021

REPOSITORIES: jPOST

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Dataset's files

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			Action	DRS
	Elmo1_Dock5_Rac1_20210216.fasta	Fasta
	SN210013_E_4ul_N1.mgf	Mgf
	SN210013_E_4ul_N1.raw	Raw
	SN210013_E_4ul_N1_FDR10.csv	Csv
	SN210013_E_4ul_N1_FDR10.mzid	Mzid

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Publications

Cryo-EM structure of the human ELMO1-DOCK5-Rac1 complex.

Kukimoto-Niino Mutsuko M Katsura Kazushige K Kaushik Rahul R Ehara Haruhiko H Yokoyama Takeshi T Uchikubo-Kamo Tomomi T Nakagawa Reiko R Mishima-Tsumagari Chiemi C Yonemochi Mayumi M Ikeda Mariko M Hanada Kazuharu K Zhang Kam Y J KYJ Shirouzu Mikako M

Science advances 20210721 30

The dedicator of cytokinesis (DOCK) family of guanine nucleotide exchange factors (GEFs) promotes cell motility, phagocytosis, and cancer metastasis through activation of Rho guanosine triphosphatases. Engulfment and cell motility (ELMO) proteins are binding partners of DOCK and regulate Rac activation. Here, we report the cryo-electron microscopy structure of the active ELMO1-DOCK5 complex bound to Rac1 at 3.8-Å resolution. The C-terminal region of ELMO1, including the pleckstrin homology (PH) ...[more]

PMID: 34290093

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