Trafficking and developmental signaling: Alix at the crossroads

Mattei, Sara; Klein, Gérard; Satre, Michel; Aubry, Laurence

doi:10.1016/j.ejcb.2006.04.002

Cited by 18 publications

(15 citation statements)

References 68 publications

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“…This observation implies that the Bro1 domains can bridge or nucleate two ESCRT-III filaments (37). ALIX also binds other important cellular components, including actin and endocytic, apoptotic, and calcium signaling machinery, although their ESCRT connections are not yet well understood (21, 38). …”

Section: Early Acting Escrt Factorsmentioning

confidence: 99%

Membrane Fission Reactions of the Mammalian ESCRT Pathway

McCullough

Colf

Sundquist³

2013

Annu. Rev. Biochem.

220

288

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The endosomal sorting complexes required for transport (ESCRT) pathway was initially defined in yeast genetic screens that identified the factors necessary to sort membrane proteins into intraluminal endosomal vesicles. Subsequent studies have revealed that the mammalian ESCRT pathway also functions in a series of other key cellular processes, including formation of extracellular microvesicles, enveloped virus budding, and the abscission stage of cytokinesis. The core ESCRT machinery comprises Bro1 family proteins and ESCRT-I, ESCRT-II, ESCRT-III, and VPS4. Site-specific adaptors recruit these soluble factors to assemble on different cellular membranes, where they carry out membrane fission reactions. ESCRT-III proteins form filaments that draw membranes together from the cytoplasmic face, and mechanistic models have been advanced to explain how ESCRT-III filaments and the VPS4 ATPase can work together to catalyze membrane fission.

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Section: Early Acting Escrt Factorsmentioning

confidence: 99%

Membrane Fission Reactions of the Mammalian ESCRT Pathway

McCullough

Colf

Sundquist³

2013

Annu. Rev. Biochem.

220

288

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“…Site-directed mutagenesis is a routine procedure with D. discoideum , and a mutant of tom1 , which encodes one of the proteins of an ESCRT-like complex in this amoeba, has already been developed (Blanc et al, 2009). Mutants of the gene encoding Alix, a protein functionally associated with ESCRT complexes, as well as of genes encoding proteins involved in autophagy are also already available (Mattei et al, 2006; Calvo-Garrido et al, 2010). Studying the capacity of these mutants and others that can be generated in the future to produce normal MLBs appears to be a good approach for shedding light on the mechanisms involved in bacteria packaging.…”

Section: Hypothesis and Perspectivesmentioning

confidence: 99%

Potential role of bacteria packaging by protozoa in the persistence and transmission of pathogenic bacteria

2014

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Many pathogenic bacteria live in close association with protozoa. These unicellular eukaryotic microorganisms are ubiquitous in various environments. A number of protozoa such as amoebae and ciliates ingest pathogenic bacteria, package them usually in membrane structures, and then release them into the environment. Packaged bacteria are more resistant to various stresses and are more apt to survive than free bacteria. New evidence indicates that protozoa and not bacteria control the packaging process. It is possible that packaging is more common than suspected and may play a major role in the persistence and transmission of pathogenic bacteria. To confirm the role of packaging in the propagation of infections, it is vital that the molecular mechanisms governing the packaging of bacteria by protozoa be identified as well as elements related to the ecology of this process in order to determine whether packaging acts as a Trojan Horse.

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“…Alix (also named AIP1) is an interacting partner of the penta‐EF‐hand Ca 2 + ‐binding protein, ALG‐2 [1–5], and acts as a multifunctional adaptor protein in various cellular functions such as cell death, receptor endocytosis, endosomal protein sorting, cell adhesion, budding of enveloped RNA viruses and development [6–9]. Alix associates through its Pro‐rich region with SH3 domains of CIN85/Ruk l /SETA [10], endophilins [11] and Src [12] at sites different from the ALG‐2 binding site [13].…”

mentioning

confidence: 99%

Brox, a novel farnesylated Bro1 domain‐containing protein that associates with charged multivesicular body protein 4 (CHMP4)

Ichioka¹,

Kobayashi²,

Katoh³

et al. 2008

The FEBS Journal

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Alix (also named AIP1) is an interacting partner of the penta-EF-hand Ca 2 + -binding protein, ALG-2 [1-5], and acts as a multifunctional adaptor protein in various cellular functions such as cell death, receptor endocytosis, endosomal protein sorting, cell adhesion, budding of enveloped RNA viruses and development 10.1111/j.1742-4658.2007.06230.x Human Brox is a newly identified 46 kDa protein that has a Bro1 domainlike sequence and a C-terminal thioester-linkage site of isoprenoid lipid (CAAX motif) (C standing for cysteine, A for generally aliphatic amino acid, and X for any amino acid). Mammalian Alix and its yeast ortholog, Bro1, are known to associate with charged multivesicular body protein 4 (CHMP4), a component of endosomal sorting complex required for transport III, via their Bro1 domains and to play roles in sorting of ubiquitinated cargoes. We investigated whether Brox has an authentic Bro1 domain on the basis of its capacity for interacting with CHMP4s. Both Strep Tac , and the mobility coincided with that of Strep-Brox C408S . The inhibitor also caused a mobility shift of endogenous Brox detected by western blotting using polyclonal antibodies to Brox, suggesting farnesylation of Brox in vivo. Fluorescence microscopic analyses revealed that Strep-Brox WT exhibited accumulation in the perinuclear area and caused a punctate pattern of FLAG-CHMP4b that was constitutively expressed in HEK293 cells. On the other hand, Strep-Brox C408S showed a diffuse pattern throughout the cell, including the nucleus, and did not cause accumulation of FLAGCHMP4b. Fluorescent signals of monomeric green fluorescent protein (mGFP)-fused Brox WT merged partly with those of Golgi markers and with those of abnormal endosomes induced by overexpression of a dominant negative mutant of AAA type ATPase SKD1 ⁄ Vps4B in HeLa cells, but such colocalization was less efficient for mGFP-Brox C408S . These results suggest a physiological significance of farnesylation of Brox in its subcellular distribution and efficient interaction with CHMP4s in vivo.Abbreviations Brox WT , wild-type Brox; CAAX motif, a thioester-linkage site of isoprenoid lipid (C standing for cysteine, A for generally aliphatic amino acid, and X for any amino acid); CHMP, charged multivesicular body protein; E-64, trans-epoxysuccinyl-L-leucylamido(4-guanidino) butane; ESCRT, endosomal sorting complex required for transport; FTI-27, farnesyltransferase inhibitor; GAPDH, glyceraldehyde-3-phosphate dehydrogenase; GFP, green fluorescent protein; GST, glutathione S-transferase; mGFP, monomeric green fluorescent protein; pAb, polyclonal antibody; PTP, protein tyrosine phosphatase; PVDF, poly(vinylidene difluoride); RabGAPLP, Rab GTPase-activating protein-like protein; Strep, StrepTactin binding sequence.

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Trafficking and developmental signaling: Alix at the crossroads

Cited by 18 publications

References 68 publications

Membrane Fission Reactions of the Mammalian ESCRT Pathway

Membrane Fission Reactions of the Mammalian ESCRT Pathway

Potential role of bacteria packaging by protozoa in the persistence and transmission of pathogenic bacteria

Brox, a novel farnesylated Bro1 domain‐containing protein that associates with charged multivesicular body protein 4 (CHMP4)

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