The YTA10–12 Complex, an AAA Protease with Chaperone-like Activity in the Inner Membrane of Mitochondria

doi:10.1016/S0092-8674(00)81271-4

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The YTA10–12 Complex, an AAA Protease with Chaperone-like Activity in the Inner Membrane of Mitochondria

Journal Article•DOI•

The YTA10–12 Complex, an AAA Protease with Chaperone-like Activity in the Inner Membrane of Mitochondria

Heike Arlt¹, Raimund Tauer¹, Horst Feldmann¹, Walter Neupert¹, Thomas Langer¹ - Show less +1 more•Institutions (1)

Ludwig Maximilian University of Munich¹

14 Jun 1996-Cell (Cell Press)-Vol. 85, Iss: 6, pp 875-885

TL;DR: It is proposed that proteolytic and chaperone-like activities in the YTA10-12 complex mediate assembly and degradation processes of membrane protein complexes and thereby exert key functions in the maintenance of membrane integrity.

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About: This article is published in Cell.The article was published on 1996-06-14 and is currently open access. It has received 301 citations till now. The article focuses on the topics: AAA proteins & Metallopeptidase activity.

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Journal Article•DOI•

Protein import into mitochondria.

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Walter Neupert¹•Institutions (1)

Ludwig Maximilian University of Munich¹

01 Jan 1997-Annual Review of Biochemistry

TL;DR: Molecular chaperones in the matrix exert multiple functions in translocation, sorting, folding, and assembly of newly imported proteins.

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Abstract: Mitochondria import many hundreds of different proteins that are encoded by nuclear genes These proteins are targeted to the mitochondria, translocated through the mitochondrial membranes, and sorted to the different mitochondrial subcompartments Separate translocases in the mitochondrial outer membrane (TOM complex) and in the inner membrane (TIM complex) facilitate recognition of preproteins and transport across the two membranes Factors in the cytosol assist in targeting of preproteins Protein components in the matrix partake in energetically driving translocation in a reaction that depends on the membrane potential and matrix-ATP Molecular chaperones in the matrix exert multiple functions in translocation, sorting, folding, and assembly of newly imported proteins

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1,079 citations

Journal Article•DOI•

Regulation of mitochondrial morphology through proteolytic cleavage of OPA1.

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Naotada Ishihara¹, Yuu Fujita¹, Toshihiko Oka¹, Katsuyoshi Mihara¹•Institutions (1)

Kyushu University¹

12 Jul 2006-The EMBO Journal

TL;DR: M mammalian mitochondrial function and morphology is regulated through processing of OPA1 in a ΔΨ‐dependent manner through proteolytic cleavage of Mgm1, the yeast homolog of O PA1.

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Abstract: The dynamin-like GTPase OPA1, a causal gene product of human dominant optic atrophy, functions in mitochondrial fusion and inner membrane remodeling. It has several splice variants and even a single variant is found as several processed forms, although their functional significance is unknown. In yeast, mitochondrial rhomboid protease regulates mitochondrial function and morphology through proteolytic cleavage of Mgm1, the yeast homolog of OPA1. We demonstrate that OPA1 variants are synthesized with a bipartite-type mitochondrial targeting sequence. During import, the matrix-targeting signal is removed and processed forms (L-isoforms) are anchored to the inner membrane in type I topology. L-isoforms undergo further processing in the matrix to produce S-isoforms. Knockdown of OPA1 induced mitochondrial fragmentation, whose network morphology was recovered by expression of L-isoform but not S-isoform, indicating that only L-isoform is fusion-competent. Dissipation of membrane potential, expression of m-AAA protease paraplegin, or induction of apoptosis stimulated this processing along with the mitochondrial fragmentation. Thus, mammalian mitochondrial function and morphology is regulated through processing of OPA1 in a ΔΨ-dependent manner.

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810 citations

Cites background from "The YTA10–12 Complex, an AAA Protea..."

...…AAA-proteases can extract TM from the membrane bilayer and translocate the unfolded hydrophilic domain in the trans-side across the membrane (Arlt et al, 1996; Leonhard et al, 1999), it is conceivable that paraplegin translocates the OPA1 L-isoforms across the membrane into the matrix side…...
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Journal Article•DOI•

The Vps4p AAA ATPase regulates membrane association of a Vps protein complex required for normal endosome function

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Markus Babst¹, Beverly Wendland¹, Eden J. Estepa¹, Scott D. Emr¹•Institutions (1)

University of California, San Diego¹

01 Jun 1998-The EMBO Journal

TL;DR: Together, the data suggest that the Vps4 ATPase catalyzes the release of an endosomal membrane‐associated class E protein complex(es) required for normal morphology and sorting activity of the endosome.

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Abstract: Vps4p is an AAA-type ATPase required for efficient transport of biosynthetic and endocytic cargo from an endosome to the lysosome-like vacuole of Saccharomyces cerevisiae. Vps4p mutants that do not bind ATP or are defective in ATP hydrolysis were characterized both in vivo and in vitro. The nucleotide-free or ADP-bound form of Vps4p existed as a dimer, whereas in the ATP-locked state, Vps4p dimers assembled into a decameric complex. This suggests that ATP hydrolysis drives a cycle of association and dissociation of Vps4p dimers/decamers. Nucleotide binding also regulated the association of Vps4p with an endosomal compartment in vivo. This membrane association required the N-terminal coiled-coil motif of Vps4p, but deletion of the coiled-coil domain did not affect ATPase activity or oligomeric assembly of the protein. Membrane association of two previously uncharacterized class E Vps proteins, Vps24p and Vps32p/Snf7p, was also affected by mutations in VPS4. Upon inactivation of a temperature-conditional vps4 mutant, Vps24p and Vps32p/Snf7p rapidly accumulated in a large membrane-bound complex. Immunofluorescence indicated that both proteins function with Vps4p at a common endosomal compartment. Together, the data suggest that the Vps4 ATPase catalyzes the release (uncoating) of an endosomal membrane-associated class E protein complex(es) required for normal morphology and sorting activity of the endosome.

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756 citations

Cites background from "The YTA10–12 Complex, an AAA Protea..."

...AAA proteins are involved in diverse cellular functions such as membrane fusion (Sec18p/NSF, Cdc48p/p97), protein degradation (YTA10-12, proteosome subunits, FtsH) and chaperone-like activities (YTA10-12, FtsH) (for reviews see Confalonieri and Duguet, 1995; Beyer, 1997; Patel and Latterich, 1998)....
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...Several AAA ATPase family members, such as Cdc48p/ p97 (Peters et al., 1990; Frohlich et al., 1995), NSF (Hanson et al., 1997) and YTA10-12 (Arlt et al., 1996), have been shown to form oligomeric complexes....
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..., 1997) and YTA10-12 (Arlt et al., 1996), have been shown to form oligomeric complexes....
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...Homotypic oligomerization has been described for several members of the AAA family and in at least two cases it was demonstrated that oligomerization requires the presence of nucleotides (NSF: Nagiec et al., 1995; Hanson et al., 1997; YTA10-12: Arlt et al., 1996)....
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Journal Article•DOI•

Spastic Paraplegia and OXPHOS Impairment Caused by Mutations in Paraplegin, a Nuclear-Encoded Mitochondrial Metalloprotease

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Giorgio Casari, Maurizio De Fusco, Sonia Ciarmatori, Massimo Zeviani, Marina Mora, Patricio Fernandez¹, Giuseppe De Michele, Alessandro Filla, Sergio Cocozza, Roberto Marconi, Alexandre Dürr², Bertrand Fontaine², Andrea Ballabio³ - Show less +9 more•Institutions (3)

Boston Children's Hospital¹, French Institute of Health and Medical Research², Vita-Salute San Raffaele University³

12 Jun 1998-Cell

TL;DR: Analysis of muscle biopsies from two patients carrying Paraplegin mutations showed typical signs of mitochondrial OXPHOS defects, thus suggesting a mechanism for neurodegeneration in HSP-type disorders.

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751 citations

Cites background from "The YTA10–12 Complex, an AAA Protea..."

...This and RCA1) form multimeric complexes (Arlt et al., 1996). molecule is highly homologous to a mitochondrial sub- These data demonstrate a mitochondrial protein declass of yeast ATPases....
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Journal Article•DOI•

AAA proteins. Lords of the ring.

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Ronald D. Vale¹•Institutions (1)

University of California, San Francisco¹

10 Jul 2000-Journal of Cell Biology

TL;DR: AAA ATPases (those associated with various cellular activities) play important roles in numerous cellular activities including proteolysis, protein folding, membrane trafficking, cytoskeletal regulation, organelle biogenesis, DNA replication, and intracellular motility.

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Abstract: AAA ATPases (those associated with various cellular activities) play important roles in numerous cellular activities including proteolysis, protein folding, membrane trafficking, cytoskeletal regulation, organelle biogenesis, DNA replication, and intracellular motility. Recent structural and

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599 citations

Cites background from "The YTA10–12 Complex, an AAA Protea..."

...The YTA10-12 complex, an AAA protease with chaperone-like activity in the inner membrane of mitochondria....
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..., 1999), and YTA10-12 (Arlt et al., 1996) with their respective protein targets....
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...The AAA Yta10-12 complex, for example, proteolyzes misfolded proteins in the mitochondrial inner membrane, but also functions in the assembly of the multisubunit ATP synthase (Arlt et al., 1996)....
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...Examples include the two different polypeptides YTA10/YTA12 protease (Arlt et al., 1996), and the six AAA proteins that come together to form the regulatory particle of the proteasome (Rubin et al....
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...Examples include the two different polypeptides YTA10/YTA12 protease (Arlt et al., 1996), and the six AAA proteins that come together to form the regulatory particle of the proteasome (Rubin et al., 1998)....
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References

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Book•

Antibodies: A Laboratory Manual

[...]

Ed Harlow, David P. Lane

01 Jan 1988

TL;DR: A second edition of Antibodies: A Laboratory Manual is being published in September 2013, Revised, extended and updated by Edward Greenfield of the Dana-Farber Cancer Center, the material has been recast with extensive new information and new chapters have been added.

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Abstract: ince its publication in 1988, Antibodies: A Laboratory Manual, by Harlow and Lane, has become a classic, an essential resource for molecular biology, immunology, and cell culture labs. In order to keep the book in print, Cold Spring Harbor Laboratory Press eventually produced the paperback edition currently available for sale. Now, after 25 years, a second edition is being published in September 2013. Revised, extended and updated by Edward Greenfield of the Dana-Farber Cancer Center, the material has been recast with extensive new information and new chapters have been added. The new edition provides clear, authoritative, current and up-to-date protocols with background information and troubleshooting advice. The book is an invaluable resource for all those engaged in antibody research and development.

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22,254 citations

Additional excerpts

...203, A–Sepharose, as previously described (Harlow and Lane, 1988)....
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Journal Article•DOI•

The ubiquitin-proteasome proteolytic pathway

[...]

Aaron Ciechanover¹•Institutions (1)

Technion – Israel Institute of Technology¹

07 Oct 1994-Cell

TL;DR: Two studies clearly demonstrate that the ubiquitin-proteasome system is involved not only in complete destruction of its protein substrates, but also in limited proteolysis and posttranslational processing in which biologically active peptides or fragments are generated.

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1,783 citations

Journal Article•DOI•

Crystal structure of the 20S proteasome from the archaeon T. acidophilum at 3.4 A resolution.

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Jan Löwe¹, Daniela Stock¹, Bing Jap¹, Peter Zwickl¹, Wolfgang Baumeister¹, Robert Huber¹ - Show less +2 more•Institutions (1)

Max Planck Society¹

28 Apr 1995-Science

TL;DR: The three-dimensional structure of the proteasome from the archaebacterium Thermoplasma acidophilum has been elucidated by x-ray crystallographic analysis by means of isomorphous replacement and cyclic averaging.

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Abstract: The three-dimensional structure of the proteasome from the archaebacterium Thermoplasma acidophilum has been elucidated by x-ray crystallographic analysis by means of isomorphous replacement and cyclic averaging. The atomic model was built and refined to a crystallographic R factor of 22.1 percent. The 673-kilodalton protease complex consists of 14 copies of two different subunits, alpha and beta, forming a barrel-shaped structure of four stacked rings. The two inner rings consist of seven beta subunits each, and the two outer rings consist of seven alpha subunits each. A narrow channel controls access to the three inner compartments. The alpha 7 beta 7 beta 7 alpha 7 subunit assembly has 72-point group symmetry. The structures of the alpha and beta subunits are similar, consisting of a core of two antiparallel beta sheets that is flanked by alpha helices on both sides. The binding of a peptide aldehyde inhibitor marks the active site in the central cavity at the amino termini of the beta subunits and suggests a novel proteolytic mechanism.

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1,532 citations

"The YTA10–12 Complex, an AAA Protea..." refers background in this paper

...…to complexes that harbor multiple proteolytic centers at promote unfolding and transfer of ubiquitinated subthe inner surface (Kessel et al., 1995; Löwe et al., 1995). strate proteins to proteolytic centers within the cavity Byanalogy, the YTA10–12 complex may provide a cavity of the 26S…...
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Book Chapter•DOI•

Evolutionary families of metallopeptidases.

[...]

Neil D. Rawlings, Alan J. Barrett

01 Jan 1995-Methods in Enzymology

780 citations