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

Manual transfer of experimentally-verified manual GO annotation data to orthologs by curator judgment of sequence similarity

GO_REF:0000033

Annotation inferences using phylogenetic trees

GO_REF:0000044

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

PMID:19570817

Molecular cloning of a novel secreted peptide, INM02, and regulation of its expression by glucose.

INM02 (EMC10) is detectable in human serum and is glucose-regulated in islets.

PMID:20680400

hHSS1: a novel secreted factor and suppressor of glioma growth located at chromosome 19q13.33.

Describes the secreted HSS1 isoform and the membrane HSM1 isoform of EMC10; HSS1 suppresses glioma growth.

PMID:22119785

Defining human ERAD networks through an integrative mapping strategy.

Affinity-MS ERAD-network mapping that first identified the EMC (including EMC10) and localized it to the ER membrane.

PMID:28931551

EMC10 (Endoplasmic Reticulum Membrane Protein Complex Subunit 10) Is a Bone Marrow-Derived Angiogenic Growth Factor Promoting Tissue Repair After Myocardial Infarction.

Secreted EMC10 is a bone marrow-derived angiogenic growth factor that stimulates endothelial cell migration and outgrowth via p38 MAPK/PAK/MK2 and promotes tissue repair after myocardial infarction.

PMID:29242231

The ER membrane protein complex is a transmembrane domain insertase.

EMC is a transmembrane domain insertase mediating tail-anchored and stop-transfer insertion.

PMID:29809151

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

PMID:30415835

EMC Is Required to Initiate Accurate Membrane Protein Topogenesis.

PMID:32439656

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

Cryo-EM structure of the human EMC, with EMC10's lumenal domain resolved; defines the signal peptide and Asn-182 glycosylation.

PMID:37196677

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

Cryo-EM structures of the EMC bound to a CaV1.2 channel assembly intermediate reveal EMC transmembrane and cytoplasmic client-docking sites and a holdase/chaperone mode; the lumenal module (EMC1/EMC4/EMC7/EMC10) shifts during client engagement.

PMID:37199759

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

Using an improved human EMC structural model, positively charged residues at the entrance of the hydrophilic vestibule act as a charge-based selectivity filter that rejects mitochondrial TA proteins and enforces the positive-inside rule; the model includes EMC7/EMC10 single-pass topology.

PMID:38517390

Structural insights into human EMC and its interaction with VDAC.

Cryo-EM apo- and VDAC-bound human EMC structures identify a gating plug within the hydrophilic vestibule and a conserved EMC-VDAC interaction at mitochondria-ER contact sites; in the VDAC1-bound state the EMC is unlikely to act as an insertase, indicating state-dependent functional switching.