{"database":"biostudies-literature","file_versions":[],"scores":null,"additional":{"submitter":["Falcone D"],"funding":["NIGMS NIH HHS","CIHR"],"pagination":["291-303"],"full_dataset_link":["https://www.ebi.ac.uk/biostudies/studies/S-EPMC3095691"],"repository":["biostudies-literature"],"omics_type":["Unknown"],"volume":["436(2)"],"pubmed_abstract":["Sss1p, an essential component of the heterotrimeric Sec61 complex in the ER (endoplasmic reticulum), is a tail-anchored protein whose precise mechanism of action is largely unknown. Tail-anchored proteins are involved in many cellular processes and are characterized by a single transmembrane sequence at or near the C-terminus. The Sec61 complex is the molecular machine through which secretory and membrane proteins translocate into and across the ER membrane. To understand the function of the tail anchor of Sss1p, we introduced mutations into the tail-anchor sequence and analysed the resulting yeast phenotypes. Point mutations in the C-terminal hydrophobic core of the tail anchor of Sss1p were identified that allowed Sss1p assembly into Sec61 complexes, but resulted in diminished growth, de"],"journal":["The Biochemical journal"],"pubmed_title":["Stability and function of the Sec61 translocation complex depends on the Sss1p tail-anchor sequence."],"pmcid":["PMC3095691"],"funding_grant_id":["R01 GM075061","R01 GM075061-06","GM75061","FRN 10490"],"pubmed_authors":["Falcone D","Coughlan CM","Brodsky JL","Henderson MP","Andrews DW","Nieuwland H"],"additional_accession":[]},"is_claimable":false,"name":"Stability and function of the Sec61 translocation complex depends on the Sss1p tail-anchor sequence.","description":"Sss1p, an essential component of the heterotrimeric Sec61 complex in the ER (endoplasmic reticulum), is a tail-anchored protein whose precise mechanism of action is largely unknown. Tail-anchored proteins are involved in many cellular processes and are characterized by a single transmembrane sequence at or near the C-terminus. The Sec61 complex is the molecular machine through which secretory and membrane proteins translocate into and across the ER membrane. To understand the function of the tail anchor of Sss1p, we introduced mutations into the tail-anchor sequence and analysed the resulting yeast phenotypes. Point mutations in the C-terminal hydrophobic core of the tail anchor of Sss1p were identified that allowed Sss1p assembly into Sec61 complexes, but resulted in diminished growth, de","dates":{"release":"2011-01-01T00:00:00Z","publication":"2011 Jun","modification":"2025-04-18T14:32:48.142Z","creation":"2019-03-27T00:41:39Z"},"accession":"S-EPMC3095691","cross_references":{"pubmed":["21355855"],"doi":["10.1042/bj20101865","10.1042/BJ20101865"]}}