The architecture of EMC reveals a path for membrane protein insertion.

Gene Ontology annotation through association of InterPro records with GO terms

Annotation inferences using phylogenetic trees

Gene Ontology annotation based on UniProtKB/Swiss-Prot Subcellular Location vocabulary mapping, accompanied by conservative changes to GO terms applied by UniProt

PMID:12975309

The secreted protein discovery initiative (SPDI), a large-scale effort to identify novel human secreted and transmembrane proteins: a bioinformatics assessment.

PMID:22119785

Defining human ERAD networks through an integrative mapping strategy.

Affinity-MS ERAD-network mapping that identified the EMC (including EMC7) in human cells and localized it to the ER membrane.

PMID:28514442

Architecture of the human interactome defines protein communities and disease networks.

PMID:28734904

Identifying novel members of the Wntless interactome through genetic and candidate gene approaches.

PMID:29242231

The ER membrane protein complex is a transmembrane domain insertase.

EMC is a transmembrane domain insertase that post-translationally inserts tail-anchored membrane proteins.

PMID:29809151

The ER membrane protein complex interacts cotranslationally to enable biogenesis of multipass membrane proteins.

The EMC engages multipass membrane protein clients cotranslationally to enable their biogenesis.

PMID:30415835

EMC Is Required to Initiate Accurate Membrane Protein Topogenesis.

The EMC sets the N-exo topology of GPCR/multipass first TMDs, initiating accurate topogenesis.

PMID:31286866

Alternative splicing of the Wnt trafficking protein, Wntless and its effects on protein-protein interactions.

PMID:32296183

A reference map of the human binary protein interactome.

PMID:32439656

Structural basis for membrane insertion by the human ER membrane protein complex.

Cryo-EM structure of the human EMC; EMC7 is a single-pass type I subunit with a large lumenal domain; the catalytic vestibule is formed by EMC3 and EMC6.

PMID:33961781

Dual proteome-scale networks reveal cell-specific remodeling of the human interactome.

PMID:35287476

The Function, Structure, and Origins of the ER Membrane Protein Complex.

Authoritative review of EMC function, structure, and evolution; places EMC7 as a single-pass subunit contributing a transmembrane helix and cytosolic loops to the dynamic front subdomain near the EMC3/EMC6 catalytic vestibule.

PMID:37199759

A selectivity filter in the ER membrane protein complex limits protein misinsertion at the ER.

EMC7 is experimentally confirmed as a type I single-pass subunit and contributes conserved hydrophobic cytosolic loops (and a C-terminal amphipathic helix) beneath the EMC hydrophilic vestibule that transiently capture substrate TMDs; EMC7 is required for biogenesis of the tail-anchored client squalene synthase (SQS).

PMID:37957425

EMC rectifies the topology of multipass membrane proteins.

The EMC post-translationally rectifies the topology of multipass membrane proteins by inserting terminal/C-terminal TMDs after release from the ribosome-Sec61 complex, a mechanism estimated to apply to ~250 diverse human multipass proteins; EMC7 participates as an EMC subunit.

PMID:32111841

Selective EMC subunits act as molecular tethers of intracellular organelles exploited during viral entry.

EMC7 (with EMC4) acts as an ER-late endosome tether supporting SV40 polyomavirus delivery to the ER; EMC7's cytosolic C-terminal tail binds the late-endosomal GTPase Rab7 and EMC7/EMC4 bind the ER SNARE syntaxin-18, and EMC7 depletion blocks SV40 infection.

PMID:38517390

Structural insights into human EMC and its interaction with VDAC.

Cryo-EM of human EMC apo and VDAC1-bound states; EMC7's transmembrane helix becomes ordered upon VDAC1 binding and contributes a substantial fraction (~one-third) of the EMC-VDAC1 interface at mitochondria-ER contact sites.

file:human/EMC7/EMC7-uniprot.txt

UniProt entry Q9NPA0 (EMC7_HUMAN), ER membrane protein complex subunit 7

Single-pass type I ER membrane EMC subunit with a lumenal beta-sandwich domain; non-catalytic; part of the EMC insertase.