2013
DOI: 10.1016/j.bbamem.2013.03.033
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Mechanism, specificity, and physiology of signal peptide peptidase (SPP) and SPP-like proteases

Abstract: Signal peptide peptidase (SPP) and the homologous SPP-like (SPPL) proteases SPPL2a, SPPL2b, SPPL2c and SPPL3 belong to the family of GxGD intramembrane proteases. SPP/SPPLs selectively cleave transmembrane domains in type II orientation and do not require additional co-factors for proteolytic activity. Orthologues of SPP and SPPLs have been identified in other vertebrates, plants, and eukaryotes. In line with their diverse subcellular localisations ranging from the ER (SPP, SPPL2c), the Golgi (SPPL3), the plas… Show more

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Cited by 122 publications
(158 citation statements)
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“…Parts of SpoIVFB and Pro-K Important for Solubilization and Complex Formation-Both the Pro (1)(2)(3)(4)(5)(6)(7)(8)(9)(10)(11)(12)(13)(14)(15)(16)(17)(18)(19)(20) and K (21-126) parts contribute to improving the solubilization of cytTMSpoIVFB-FLAG 2 E44Q from membranes with 1% DM (Fig. 3, D and E).…”
Section: Solubilization Of An Immp⅐substratementioning
confidence: 99%
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“…Parts of SpoIVFB and Pro-K Important for Solubilization and Complex Formation-Both the Pro (1)(2)(3)(4)(5)(6)(7)(8)(9)(10)(11)(12)(13)(14)(15)(16)(17)(18)(19)(20) and K (21-126) parts contribute to improving the solubilization of cytTMSpoIVFB-FLAG 2 E44Q from membranes with 1% DM (Fig. 3, D and E).…”
Section: Solubilization Of An Immp⅐substratementioning
confidence: 99%
“…Dysfunction of ␥-secretase contributes to the pathogenesis of Alzheimer disease (8) and many other diseases (7). Aspartyl IPs also include preflagellin and prepilin peptidases involved in bacterial pathogenesis (9), and signal peptide peptidases, which facilitate the clearance of signal peptides from membranes, participate in viral infection, and generate small peptides as signal molecules for immune systems (10,11). IMMPs also play critical roles in a wide variety of biological functions.…”
mentioning
confidence: 99%
“…Although it may be tempting to speculate that this is a conserved mechanism for all I-CLiPs, rhomboid is the only family of I-CLiPs that does not require prior activation of substrate through an initial cleavage by another protease (8). Specifically, site-2 protease substrates must be first cleaved by site-1 protease (9), signal peptide peptidase substrates are first cleaved by signal peptidase (10), and ectodomain shedding by α-or β-secretase is required before γ-secretase cleavage of its substrates (11,12). These facts suggest that the diverse families of I-CLiPs likely have evolved fundamentally different mechanisms by which they recognize and cleave their substrates.…”
mentioning
confidence: 99%
“…SPP cleaves endoplasmic reticulum-resident substrates, which include, among others, signal peptides (14) and tail-anchored endoplasmic reticulum proteins (15). At least SPP and SPPL2b cleave type 2 membrane protein stubs following shedding (13,16,17). Similar to some ␥-secretase substrates, ICDs liberated from their membrane anchors by SPPL2a/SPPL2b have been reported to regulate gene expression (17,18).…”
mentioning
confidence: 99%
“…However, in many cases ␥-secretase processing may contribute to the final degradation of membrane fragments (12). Whereas ␥-secretase exclusively accepts type 1 substrates, type 2-oriented membrane fragments are cleaved by I-CLiPs belonging to the signal peptide peptidase (SPP) and SPP-like (SPPL) subfamily of mammalian GXGD proteases (13). SPP/SPPLs share structural features with PSs, including the characteristic overall topology and the essential catalytic GXGD motif (14).…”
mentioning
confidence: 99%