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

GO_REF:0000120

Combined Automated Annotation using Multiple IEA Methods

PMID:22119785

Defining human ERAD networks through an integrative mapping strategy.

Affinity-MS ERAD-network mapping that first identified the EMC (including EMC1) in human cells and localized it to the ER membrane.

PMID:28246125

ZMPSTE24 defends against influenza and other pathogenic viruses.

Antiviral study of ZMPSTE24/IFITM; EMC1 appears only as a co-purifying generic protein-containing complex component (MGI IDA), not as a functional subject.

PMID:29242231

The ER membrane protein complex is a transmembrane domain insertase.

The EMC is a transmembrane domain insertase that post-translationally inserts tail-anchored membrane proteins; reconstituted in liposomes.

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 the first TMD of GPCRs and other multipass proteins, cooperating with Sec61.

PMID:32353859

A SARS-CoV-2 protein interaction map reveals targets for drug repurposing.

PMID:32439656

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

Cryo-EM structure of the human EMC; substrate insertion occurs via an enclosed hydrophilic vestibule formed by EMC3 and EMC6, while EMC1 is the large lumenal scaffold subunit.

PMID:33060197

Comparative host-coronavirus protein interaction networks reveal pan-viral disease mechanisms.

PMID:36217030

A comprehensive SARS-CoV-2-human protein-protein interactome reveals COVID-19 pathobiology and potential host therapeutic targets.

PMID:37196677

EMC chaperone-Ca(V) structure reveals an ion channel assembly intermediate.

Cryo-EM structures of human EMC bound to a CaV1.2-CaVbeta3 assembly intermediate define EMC client-binding sites (transmembrane and cytoplasmic docks), with EMC1 contributing to the TM dock that engages the channel; EMC acts as a holdase/chaperone whose binding is mutually exclusive with CaValpha2delta, indicating an ordered hand-off during channel assembly.

PMID:37199759

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

Mapping of a tail-anchored substrate's path through the EMC reveals cytosolic capture by methionine-rich loops and insertion through a hydrophilic vestibule whose positively charged entrance acts as a charge-repulsion selectivity filter that rejects mitochondrial TA proteins and enforces the positive-inside topology rule.

PMID:38517390

Structural insights into human EMC and its interaction with VDAC.

Cryo-EM structures of human EMC in apo and VDAC-bound states (3.47 A and 3.32 A) identify a gating plug within the hydrophilic vestibule and a conserved EMC-VDAC interaction at mitochondria-ER contact sites; the VDAC-bound state appears not to be insertion-competent, supporting EMC multifunctionality.

PMID:38784058

Tribal Founder EMC1 Variant in 5 Kuwaiti Families Expands Phenotypic Spectrum of EMC1-Related Disorder.

Eight individuals from 5 Kuwaiti families homozygous for the EMC1 c.245C>T (p.Thr82Met) variant present with CAVIPMR (OMIM

PMID:40753078

The EMC acts as a chaperone for membrane proteins.

Interactomics and model-protein studies define an EMC chaperone function distinct from its insertase activity; the EMC engages client transmembrane domains via its EMC1 subunit and modulates their orientation in the lipid bilayer, with productive assembly reducing binding to the EMC chaperone site.