Endoplasmic reticulum membrane localization of Rce1p and Ste24p, yeast proteases involved in carboxyl-terminal CAAX protein processing and amino-terminal a-factor cleavage
about
Cloning and characterization of a mammalian prenyl protein-specific proteaseIsoprenylcysteine carboxyl methyltransferase deficiency in miceMutational analysis of the ras converting enzyme reveals a requirement for glutamate and histidine residuesHuman ZMPSTE24 disease mutations: residual proteolytic activity correlates with disease severityDual roles for Ste24p in yeast a-factor maturation: NH2-terminal proteolysis and COOH-terminal CAAX processingDifferential localization of Rho GTPases in live cells: regulation by hypervariable regions and RhoGDI bindingMechanism of farnesylated CAAX protein processing by the intramembrane protease Rce1Erf2, a novel gene product that affects the localization and palmitoylation of Ras2 in Saccharomyces cerevisiae.Skp1p and the F-box protein Rcy1p form a non-SCF complex involved in recycling of the SNARE Snc1p in yeastSmall-molecule inhibitors of the Rce1p CaaX proteaseYeast as a tractable genetic system for functional studies of the insulin-degrading enzyme.The SNARE Ykt6 is released from yeast vacuoles during an early stage of fusion.The multispanning membrane protein Ste24p catalyzes CAAX proteolysis and NH2-terminal processing of the yeast a-factor precursor.A novel Ras inhibitor, Eri1, engages yeast Ras at the endoplasmic reticulum.The CaaX proteases, Afc1p and Rce1p, have overlapping but distinct substrate specificities.Ste24p Mediates Proteolysis of Both Isoprenylated and Non-prenylated Oligopeptides.The yeast a-factor transporter Ste6p, a member of the ABC superfamily, couples ATP hydrolysis to pheromone export.Chemical inhibition of CaaX protease activity disrupts yeast Ras localization.Analysis of prelamin A biogenesis reveals the nucleus to be a CaaX processing compartmentDisruption of the mouse Rce1 gene results in defective Ras processing and mislocalization of Ras within cellsCloning and characterization of a 72-kDa inositol-polyphosphate 5-phosphatase localized to the Golgi networkTargeted inactivation of the isoprenylcysteine carboxyl methyltransferase gene causes mislocalization of K-Ras in mammalian cellsYeast genes controlling responses to topogenic signals in a model transmembrane protein.Modulation of the inhibitor properties of dipeptidyl (acyloxy)methyl ketones toward the CaaX proteases.Postprenylation CAAX processing is required for proper localization of Ras but not Rho GTPasesTherapeutic intervention based on protein prenylation and associated modificationsMembrane trafficking of heterotrimeric G proteins via the endoplasmic reticulum and GolgiRequirements for efficient proteolytic cleavage of prelamin A by ZMPSTE24.Absence of the CAAX endoprotease Rce1: effects on cell growth and transformation.Prelamin A, Zmpste24, misshapen cell nuclei, and progeria--new evidence suggesting that protein farnesylation could be important for disease pathogenesis.Structural analysis of protein prenyl groups and associated C-terminal modificationsInsider information: how palmitoylation of Ras makes it a signaling double agent.Signaling at the Golgi.Membrane targeting of Rab GTPases is influenced by the prenylation motifExpansion of type II CAAX proteases reveals evolutionary origin of γ-secretase subunit APH-1A striking quality control subcompartment in Saccharomyces cerevisiae: the endoplasmic reticulum-associated compartment.Photoaffinity labeling of Ras converting enzyme using peptide substrates that incorporate benzoylphenylalanine (Bpa) residues: improved labeling and structural implications8-Hydroxyquinoline-based inhibitors of the Rce1 protease disrupt Ras membrane localization in human cells.Palmitoylation and plasma membrane localization of Ras2p by a nonclassical trafficking pathway in Saccharomyces cerevisiae.Quantitative structure-activity relationship (QSAR) of indoloacetamides as inhibitors of human isoprenylcysteine carboxyl methyltransferase.
P2860
Q22009066-16270027-A264-434C-B39D-2A69B9B531AAQ24290644-EFE74485-82FB-4E27-87C6-D7C04533DDF4Q24611091-4B4247E4-7474-445F-B706-AA6CEF102E18Q24611268-6B611686-FC74-4869-ABF9-4ADF87D63212Q24670437-2B33B366-09B7-46E0-9403-E32BA6876822Q24674800-7AB0F357-74A6-4129-A373-AB0492F2238AQ27680718-8CB6DE54-7651-42EA-86D6-FFA9F03CFE9BQ27930162-A8AF619D-8454-41E7-BE9B-6DD618E487C1Q27931687-A3E6F7FD-C68E-415C-9EB2-4A220D30AFF4Q27932239-B8992107-58FA-4297-86A8-6C2F5520E614Q27932546-E2879CB9-3EE0-48CE-A982-65C2290A4B51Q27934973-38E97A19-5738-44AB-87DC-A685C0E8FE8AQ27935263-B0E41886-B2F5-4D80-8F64-DD13980190F6Q27935341-FEB09AC7-7CA4-4981-9AB6-E31B146D466FQ27935653-197F9C62-97D0-4EF7-AD7B-DCFE8AFAD20FQ27935867-61B7517A-D040-4C88-8E04-B04E16041C33Q27936552-4EFAB30C-1F6C-4D25-86B3-C91C9E6DA7EBQ27937343-86A94FDB-1B96-4E9C-9DDA-6028DECE7D0FQ27939423-0947E4C7-F727-42AB-A8AB-90ECB664CCA0Q28506731-4BEB86D0-3D0E-4E0D-AC67-FC8C80BC601EQ28512973-705B3EFC-FD4F-42C1-8B6D-F8C2CA36FA24Q28586789-E4955279-4199-4D70-811D-B8661133E9FEQ31048364-194F498A-C467-41C2-960E-13BB631192D3Q33653120-18C1475F-8A71-4CE8-9AFA-751BD8E85D83Q33734499-D00B0CB6-440C-463F-86D2-2DC777E66BDEQ33943379-8C946B69-55E8-436A-9AD1-5B6CFE01B314Q34061239-9F3AD37F-281C-4856-8885-C7F7E9B5D47BQ34166555-55CDC9E1-FC0A-43ED-9C8E-83CDBFC046FFQ34290291-509A6DB6-D453-48CB-B641-A54F94ED579DQ34457223-242A1258-74D1-4921-AF9D-4F07B3B14A2CQ34537317-A74CCA91-1A7E-44F9-99C4-CBEA877F8A7AQ34931245-3542FC7C-7839-4BB8-BE57-C775852E7818Q35006511-2B1A43BE-A086-45C0-A638-7746AFB17376Q35153478-C9BFEFF0-A358-46E0-98FB-2BF7709ECDA4Q35161860-84C61083-F0E8-4878-A647-6D17A66682A7Q35803161-47DC3170-C9BA-4112-98AA-B4DFAFD7A8D9Q35870327-4BD7C901-8F27-4B12-A2B9-A9BDB09F8EF8Q35878817-6CAE7C1A-816F-4908-A990-9145EB26FDDEQ35920861-201D16CD-2225-4950-9A73-E97135911562Q35928477-8C2FF609-78DC-40F6-B91F-D88025AA5B5A
P2860
Endoplasmic reticulum membrane localization of Rce1p and Ste24p, yeast proteases involved in carboxyl-terminal CAAX protein processing and amino-terminal a-factor cleavage
description
1998 nî lūn-bûn
@nan
1998 թուականի Սեպտեմբերին հրատարակուած գիտական յօդուած
@hyw
1998 թվականի սեպտեմբերին հրատարակված գիտական հոդված
@hy
1998年の論文
@ja
1998年論文
@yue
1998年論文
@zh-hant
1998年論文
@zh-hk
1998年論文
@zh-mo
1998年論文
@zh-tw
1998年论文
@wuu
name
Endoplasmic reticulum membrane ...... ino-terminal a-factor cleavage
@ast
Endoplasmic reticulum membrane ...... ino-terminal a-factor cleavage
@en
Endoplasmic reticulum membrane ...... no-terminal a-factor cleavage.
@nl
type
label
Endoplasmic reticulum membrane ...... ino-terminal a-factor cleavage
@ast
Endoplasmic reticulum membrane ...... ino-terminal a-factor cleavage
@en
Endoplasmic reticulum membrane ...... no-terminal a-factor cleavage.
@nl
prefLabel
Endoplasmic reticulum membrane ...... ino-terminal a-factor cleavage
@ast
Endoplasmic reticulum membrane ...... ino-terminal a-factor cleavage
@en
Endoplasmic reticulum membrane ...... no-terminal a-factor cleavage.
@nl
P2093
P2860
P3181
P356
P1476
Endoplasmic reticulum membrane ...... ino-terminal a-factor cleavage
@en
P2093
K Fujimura-Kamada
S Michaelis
W K Schmidt
P2860
P304
P3181
P356
10.1073/PNAS.95.19.11175
P407
P577
1998-09-15T00:00:00Z