<HashMap><database>biostudies-literature</database><scores/><additional><submitter>Yan R</submitter><funding>David and Lucile Packard Foundation</funding><funding>NIGMS NIH HHS</funding><funding>NIGMS</funding><pagination>512-525.e8</pagination><full_dataset_link>https://www.ebi.ac.uk/biostudies/studies/S-EPMC8891076</full_dataset_link><repository>biostudies-literature</repository><omics_type>Unknown</omics_type><volume>57(4)</volume><pubmed_abstract>The endoplasmic reticulum (ER)-to-Golgi transport is critical to protein secretion and intracellular sorting. Here, we report a highly elongated tubular ER-Golgi intermediate compartment (t-ERGIC) that selectively expedites the ER-to-Golgi transport for soluble cargoes of the receptor SURF4. Lacking the canonical ERGIC marker ERGIC-53 yet positive for the small GTPases Rab1A/B, the t-ERGIC is further marked by its extraordinarily elongated and thinned shape. With its large surface-to-volume ratio, high intracellular traveling speeds, and ER-Golgi recycling capabilities, the t-ERGIC accelerates the trafficking of SURF4-bound cargoes. The biogenesis and cargo selectivity of t-ERGIC both depend on SURF4, which recognizes the N terminus of soluble cargoes and co-clusters with the selected carg</pubmed_abstract><journal>Developmental cell</journal><pubmed_title>SURF4-induced tubular ERGIC selectively expedites ER-to-Golgi transport.</pubmed_title><pmcid>PMC8891076</pmcid><funding_grant_id>DP2 GM132681</funding_grant_id><pubmed_authors>Xu K</pubmed_authors><pubmed_authors>Chen K</pubmed_authors><pubmed_authors>Wang B</pubmed_authors><pubmed_authors>Yan R</pubmed_authors></additional><is_claimable>false</is_claimable><name>SURF4-induced tubular ERGIC selectively expedites ER-to-Golgi transport.</name><description>The endoplasmic reticulum (ER)-to-Golgi transport is critical to protein secretion and intracellular sorting. Here, we report a highly elongated tubular ER-Golgi intermediate compartment (t-ERGIC) that selectively expedites the ER-to-Golgi transport for soluble cargoes of the receptor SURF4. Lacking the canonical ERGIC marker ERGIC-53 yet positive for the small GTPases Rab1A/B, the t-ERGIC is further marked by its extraordinarily elongated and thinned shape. With its large surface-to-volume ratio, high intracellular traveling speeds, and ER-Golgi recycling capabilities, the t-ERGIC accelerates the trafficking of SURF4-bound cargoes. The biogenesis and cargo selectivity of t-ERGIC both depend on SURF4, which recognizes the N terminus of soluble cargoes and co-clusters with the selected carg</description><dates><release>2022-01-01T00:00:00Z</release><publication>2022 Feb</publication><modification>2026-05-28T08:07:33.052Z</modification><creation>2025-04-25T17:02:44.554Z</creation></dates><accession>S-EPMC8891076</accession><cross_references><pubmed>35051356</pubmed><doi>10.1016/j.devcel.2021.12.018</doi></cross_references></HashMap>