Import and assembly of proteins into mitochondria of mammalian cells

Hoogenraad, Nicholas J.; Ward, L. A.; Ryan, Michael

doi:10.1016/s0167-4889(02)00268-9

Cited by 152 publications

(105 citation statements)

References 95 publications

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“…In humans and other animals, the mitochondrial genome is small; in humans it codes for only 13 proteins so that almost all of the 1000 proteins that constitute the mitochondria are synthesized on ribosomes in the cytosol and targeted to mitochondria posttranslationally [41]. Mitochondrial targeting information is coded in hydrophobic and basic residues, often present at the N-terminus in the form of a basic, amphipathic helix referred to as a presequence.…”

Section: Box 2 Protein Import Into Mitochondria: Animals and Fungimentioning

confidence: 99%

“…Mitochondrial targeting information is coded in hydrophobic and basic residues, often present at the N-terminus in the form of a basic, amphipathic helix referred to as a presequence. Such presequences are 30-50 residues long and are proteolytically removed by peptidases: the matrix processing peptidase (MPP) or inner membrane located peptidase (IMP), once the imported protein has reached its final destination within the mitochondrion [2,35,41].…”

Section: Box 2 Protein Import Into Mitochondria: Animals and Fungimentioning

confidence: 99%

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The direct route: a simplified pathway for protein import into the mitochondrion of trypanosomes

Schneider

Bursać

Lithgow

2008

Trends in Cell Biology

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Section: Box 2 Protein Import Into Mitochondria: Animals and Fungimentioning

confidence: 99%

Section: Box 2 Protein Import Into Mitochondria: Animals and Fungimentioning

confidence: 99%

The direct route: a simplified pathway for protein import into the mitochondrion of trypanosomes

Schneider

Bursać

Lithgow

2008

Trends in Cell Biology

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“…The TOM machinery consists of two import receptors, Tom20 and Tom70, and a number of other subunits that are ar- ranged in a tightly bound complex termed the "general import pore" (Pfanner and Geissler, 2001;Endo and Kohda, 2002;Hoogenraad et al, 2002;Stojanovski et al, 2003). Tom20 binds preproteins with both N-terminal presequences as well as internal targeting signals, whereas Tom70 preferentially binds preproteins with internal targeting information (Brix et al, 1997).…”

Section: Introductionmentioning

confidence: 99%

An Internal EELD Domain Facilitates Mitochondrial Targeting of Mcl-1 via a Tom70-dependent Pathway

Chou

Lee

Yang-Yen

2006

MBoC

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“…The central entry gate for almost all nuclear-encoded mitochondrial proteins is the translocase of the outer mitochondrial membrane (TOM complex) (for a detailed review see refs. [2][3][4]. After passing through this complex, the precursor proteins follow different routes to their final destinations within the organelle.…”

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confidence: 99%

Nanoscale distribution of mitochondrial import receptor Tom20 is adjusted to cellular conditions and exhibits an inner-cellular gradient

Wurm

Neumann

Lauterbach

et al. 2011

Proc. Natl. Acad. Sci. U.S.A.

147

114

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The translocase of the mitochondrial outer membrane (TOM) complex is the main import pore for nuclear-encoded proteins into mitochondria, yet little is known about its spatial distribution within the outer membrane. Super-resolution stimulated emission depletion microscopy was used to determine quantitatively the nanoscale distribution of Tom20, a subunit of the TOM complex, in more than 1,000 cells. We demonstrate that Tom20 is located in clusters whose nanoscale distribution is finely adjusted to the cellular growth conditions as well as to the specific position of a cell within a microcolony. The density of the clusters correlates to the mitochondrial membrane potential. The distributions of clusters of Tom20 and of Tom22 follow an inner-cellular gradient from the perinuclear to the peripheral mitochondria. We conclude that the nanoscale distribution of the TOM complex is finely adjusted to the cellular conditions, resulting in distribution gradients both within single cells and between adjacent cells.M itochondria are essential organelles in eukaryotes, occupying a central role in cellular energy metabolism. The activity of mitochondria is adapted to changing cellular conditions: It has been suggested that short-term variations in energy demand may be compensated without modification of the mitochondrial enzyme content, but modulation of the mitochondrial protein content has been observed during long-term adaptations (1).In human cells, only 13 proteins are encoded by the mitochondrial genome; most mitochondrial proteins are synthesized as precursor proteins in the cytosol and are imported into the organelle. The central entry gate for almost all nuclear-encoded mitochondrial proteins is the translocase of the outer mitochondrial membrane (TOM complex) (for a detailed review see refs. 2-4). After passing through this complex, the precursor proteins follow different routes to their final destinations within the organelle. The TOM complex consists of the receptors Tom20, Tom22, and Tom70, the channel-forming protein Tom40, and several small, associated subunits. Tom20 is the initial recognition site for preproteins with presequences (5, 6) and transfers the preproteins to the central receptor, Tom22 (7, 8). From there, the precursors are inserted into the Tom40 channel.Although the components of the TOM complex and their molecular functions have been described in great detail, little is known about the distributions of the TOM complexes within the outer membrane, and even less is known about the spatial distributions of the complexes with respect to changing mitochondrial activities. The optical resolution in far-field fluorescence microscopy, arguably the most suitable approach for studying quantitatively the distribution of protein complexes in mitochondria of intact cells, is limited to ∼200 nm by diffraction (9). This resolution is not sufficient to resolve individual TOM complexes in mitochondria (10, 11). To overcome this problem, we used stimulated emission depletion (STED) super-resolution microscopy (...

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Import and assembly of proteins into mitochondria of mammalian cells

Cited by 152 publications

References 95 publications

The direct route: a simplified pathway for protein import into the mitochondrion of trypanosomes

The direct route: a simplified pathway for protein import into the mitochondrion of trypanosomes

An Internal EELD Domain Facilitates Mitochondrial Targeting of Mcl-1 via a Tom70-dependent Pathway

Nanoscale distribution of mitochondrial import receptor Tom20 is adjusted to cellular conditions and exhibits an inner-cellular gradient

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