ArticleThe Journal of biological chemistry2008
An internal signal sequence directs intramembrane proteolysis of a cellular immunoglobulin domain protein.
Article in The Journal of biological chemistry, 2008. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 20 papers.
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The abstract states no effect estimate the extractor could read, or names no intervention and outcome on the map, so this paper lights no cell and moves no belief. It is still indexed, cited and linked below.
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Who cites it
20 citing papers in PubMed, 38 citations in OpenAlex.
- A novel variant ofClinical pediatric endocrinology : case reports and clinical investigations : official journal of the Japanese Society for Pediatric Endocrinology · 2024Article
- IGSF1 Deficiency Leads to Reduced TSH Production Independent of Alterations in Thyroid Hormone Action in Male Mice.Endocrinology · 2022Article
- The extant immunoglobulin superfamily, member 1 gene results from an ancestral gene duplication in eutherian mammals.PloS one · 2022Article
- A Case of Congenital Central Hypothyroidism Caused by a Novel Variant (Gln1255Ter) inJournal of clinical research in pediatric endocrinology · 2021Article
- IGSF1 Does Not Regulate Spermatogenesis or Modify FSH Synthesis in Response to Inhibins or Activins.Journal of the Endocrine Society · 2021Article
- IGSF1 Deficiency Results in Human and Murine Somatotrope Neurosecretory Hyperfunction.The Journal of clinical endocrinology and metabolism · 2020Article
- Unraveling the LRC Evolution in Mammals: IGSF1 and A1BG Provide the Keys.Genome biology and evolution · 2019Article
- A novel IGSF1 mutation in a large Irish kindred highlights the need for familial screening in the IGSF1 deficiency syndrome.Clinical endocrinology · 2018Article
- From Consternation to Revelation: Discovery of a Role for IGSF1 in Pituitary Control of Thyroid Function.Journal of the Endocrine Society · 2018Review
- TRH Action Is Impaired in Pituitaries of Male IGSF1-Deficient Mice.Endocrinology · 2017Article
- The short mRNA isoform of the immunoglobulin superfamily, member 1 gene encodes an intracellular glycoprotein.PloS one · 2017Article
- Genetics of Combined Pituitary Hormone Deficiency: Roadmap into the Genome Era.Endocrine reviews · 2016Review
- Characterization of a Non-Canonical Signal Peptidase Cleavage Site in a Replication Protein from Tomato Ringspot Virus.PloS one · 2016Article
- Recent advances in central congenital hypothyroidism.The Journal of endocrinology · 2015Review
- Differential Inhibition of Signal Peptide Peptidase Family Members by Established γ-Secretase Inhibitors.PloS one · 2015Article
- Neonatal screening and a new cause of congenital central hypothyroidism.Annals of pediatric endocrinology & metabolism · 2014Review
- IGSF1 deficiency syndrome: A newly uncovered endocrinopathy.Rare diseases (Austin, Tex.) · 2013Article
- Loss-of-function mutations in IGSF1 cause an X-linked syndrome of central hypothyroidism and testicular enlargement.Nature genetics · 2012Article
- Signal peptide peptidases are expressed in the shoot apex of rice, localized to the endoplasmic reticulum.Plant cell reports · 2009Article
- Signal peptide peptidases: a family of intramembrane-cleaving proteases that cleave type 2 transmembrane proteins.Seminars in cell & developmental biology · 2009Review
Corrections and comments
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Authors and funding
5 authors at 2 institutions in 2 countries.
Funding
No grant is acknowledged in the PubMed record.
Abstract
Precursor proteolysis is a crucial mechanism for regulating protein structure and function. Signal peptidase (SP) is an enzyme with a well defined role in cleaving N-terminal signal sequences but no demonstrated function in the proteolysis of cellular precursor proteins. We provide evidence that SP mediates intraprotein cleavage of IgSF1, a large cellular Ig domain protein that is processed into two separate Ig domain proteins. In addition, our results suggest the involvement of signal peptide peptidase (SPP), an intramembrane protease, which acts on substrates that have been previously cleaved by SP. We show that IgSF1 is processed through sequential proteolysis by SP and SPP. Cleavage is directed by an internal signal sequence and generates two separate Ig domain proteins from a polytopic precursor. Our findings suggest that SP and SPP function are not restricted to N-terminal signal sequence cleavage but also contribute to the processing of cellular transmembrane proteins.
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Registered trials
Read under generation 80e0d062 · epoch 390. Bibliography from PubMed, PubMed Central and OpenAlex; grants from NIH RePORTER; trial links from ClinicalTrials.gov; estimates, votes and beliefs from the OpenQuestion graph.