The Yip1 domain family is a group of proteins involved in regulating secretory traffic in eukaryotes. The family consists of four members in yeast and nine members in humans. Family members have a shared architecture containing five transmembrane domains.
Yip1 domain family members are found in all eukaryotes.[1] The budding yeast Saccharomyces cerevisiae has four Yip1 domain family members: Yif1p, Yip1p, Yip4p, and Yip5p.[1] The amino acid sequence of the Yip domain family members divides them into two groups, called α-subunits and β-subunits. The α-subunits – in yeast Yip1p and Yip4p – are more closely related to each other than they are to the β-subunits, Yip5p and Yif1p. In mammals, both groups are expanded, with α-subunits YipF4, YipF5, YipF6, and YipF7; as well as β-subunits Yif1A, Yif1B, YipF1, YipF2, and YipF3.[1]
Functionedit
Localization of Yip1 domain family members
Yip1 domain family members localize to the Golgi apparatus, where they interact with each other to form complexes involved in trafficking cargo within the Golgi, and/or between the endoplasmic reticulum and Golgi.[2] The Yip1 domain family members are widely distributed throughout the body – with the exception of YipF7 found primarily in the skeletal muscle and tongue, while YipF1A is predominantly in the liver.[2] Within the cell, the different Yip family members have slightly different localizations, with YipF5, YipF7, Yif1A, and Yif1B (in yeast Yip1p and Yif1p) at the margin of the endoplasmic reticulum and Golgi; YipF3 and YipF4 at the cis-Golgi; and YipF1, YipF2, and Yipf6 (in yeast Yip4p and Yip5p) at the trans-Golgi.[1]
YipF1 was conditionally knocked-out in mice with no observable effect.[3]
A non-functional version of YipF6 exacerbated intestinal inflammation in mice, and sometimes resulted in spontaneous intestinal inflammatory disease.[4]
Structureedit
Each Yip1 domain family protein contains five transmembrane domains, with the N-terminus exposed to the cytosol and the C-terminus to the Golgi apparatus lumen.[1] Yip1 domain family members are thought to interact with a partner, with two molecules of each partner forming an active tetramer complex with 20 transmembrane segments.[1]
Referencesedit
^ abcdefShaik S, Pandey H, Thirumalasetti SK, Nakamura N (2019). "Characteristics and Functions of the Yip1 Domain Family (YIPF), Multi-Span Transmembrane Proteins Mainly Localized to the Golgi Apparatus". Front Cell Dev Biol. 7: 130. doi:10.3389/fcell.2019.00130. PMC6682643. PMID 31417902.
^ abAttwood MM, Schiöth HB (2021). "Characterization of Five Transmembrane Proteins: With Focus on the Tweety, Sideroflexin, and YIP1 Domain Families". Front Cell Dev Biol. 9: 708754. doi:10.3389/fcell.2021.708754. PMC8327215. PMID 34350187.
^Gerdin AK (2010). "The Sanger Mouse Genetics Programme: High throughput characterisation of knockout mice". Acta Ophthalmologica. 88 (S248). doi:10.1111/j.1755-3768.2010.4142.x. S2CID 85911512.
^Moresco, Eva Marie Y.; Brandl, Katherina (January 2013). "Linking membrane trafficking and intestinal homeostasis". Tissue Barriers. 1 (1): e23119. doi:10.4161/tisb.23119. PMC3875636. PMID 24665373.
April 15, 2024
yip1, domain, family, group, proteins, involved, regulating, secretory, traffic, eukaryotes, family, consists, four, members, yeast, nine, members, humans, family, members, have, shared, architecture, containing, five, transmembrane, domains, architecture, pro. The Yip1 domain family is a group of proteins involved in regulating secretory traffic in eukaryotes The family consists of four members in yeast and nine members in humans Family members have a shared architecture containing five transmembrane domains Architecture of Yip1 domain family proteins Contents 1 Evolution 2 Function 3 Structure 4 ReferencesEvolution editYip1 domain family members are found in all eukaryotes 1 The budding yeast Saccharomyces cerevisiae has four Yip1 domain family members Yif1p Yip1p Yip4p and Yip5p 1 The amino acid sequence of the Yip domain family members divides them into two groups called a subunits and b subunits The a subunits in yeast Yip1p and Yip4p are more closely related to each other than they are to the b subunits Yip5p and Yif1p In mammals both groups are expanded with a subunits YipF4 YipF5 YipF6 and YipF7 as well as b subunits Yif1A Yif1B YipF1 YipF2 and YipF3 1 Function edit nbsp Localization of Yip1 domain family membersYip1 domain family members localize to the Golgi apparatus where they interact with each other to form complexes involved in trafficking cargo within the Golgi and or between the endoplasmic reticulum and Golgi 2 The Yip1 domain family members are widely distributed throughout the body with the exception of YipF7 found primarily in the skeletal muscle and tongue while YipF1A is predominantly in the liver 2 Within the cell the different Yip family members have slightly different localizations with YipF5 YipF7 Yif1A and Yif1B in yeast Yip1p and Yif1p at the margin of the endoplasmic reticulum and Golgi YipF3 and YipF4 at the cis Golgi and YipF1 YipF2 and Yipf6 in yeast Yip4p and Yip5p at the trans Golgi 1 YipF1 was conditionally knocked out in mice with no observable effect 3 A non functional version of YipF6 exacerbated intestinal inflammation in mice and sometimes resulted in spontaneous intestinal inflammatory disease 4 Structure editEach Yip1 domain family protein contains five transmembrane domains with the N terminus exposed to the cytosol and the C terminus to the Golgi apparatus lumen 1 Yip1 domain family members are thought to interact with a partner with two molecules of each partner forming an active tetramer complex with 20 transmembrane segments 1 References edit a b c d e f Shaik S Pandey H Thirumalasetti SK Nakamura N 2019 Characteristics and Functions of the Yip1 Domain Family YIPF Multi Span Transmembrane Proteins Mainly Localized to the Golgi Apparatus Front Cell Dev Biol 7 130 doi 10 3389 fcell 2019 00130 PMC 6682643 PMID 31417902 a b Attwood MM Schioth HB 2021 Characterization of Five Transmembrane Proteins With Focus on the Tweety Sideroflexin and YIP1 Domain Families Front Cell Dev Biol 9 708754 doi 10 3389 fcell 2021 708754 PMC 8327215 PMID 34350187 Gerdin AK 2010 The Sanger Mouse Genetics Programme High throughput characterisation of knockout mice Acta Ophthalmologica 88 S248 doi 10 1111 j 1755 3768 2010 4142 x S2CID 85911512 Moresco Eva Marie Y Brandl Katherina January 2013 Linking membrane trafficking and intestinal homeostasis Tissue Barriers 1 1 e23119 doi 10 4161 tisb 23119 PMC 3875636 PMID 24665373 Retrieved from https en wikipedia org w index php title Yip1 domain family amp oldid 1095406085, wikipedia, wiki, book, books, library,
