Process elongation of oligodendrocytes is promoted by the Kelch‐related actin‐binding protein Mayven

Jiang, Shuxian; Avraham, Hava; Park, Shin-Young; Kim, Tae-Aug; Bu, Xia; Seng, Seyha; Avraham, Shalom

doi:10.1111/j.1471-4159.2004.02946.x

Cited by 30 publications

(42 citation statements)

References 46 publications

(76 reference statements)

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“…Oligodendroglial process network formation, characterized by the generation and remodeling of higher order branches and interconnections, is initialized by well-coordinated changes in the organization of the actin cytoskeleton (Wilson and Brophy, 1989;Richter-Landsberg, 2000;Song et al, 2001;Liu et al, 2003;Jiang et al, 2005;Williams et al, 2005;Brockschnieder et al, 2006;Nielsen et al, 2006). In non-process bearing, migratory cells such actin cytoskeletal changes are to a large extent controlled by two interdependent mechanisms: 1) modifications of the extracellular environment and 2) the recruitment, retention and dissociation of molecules from focal adhesions, i.e.…”

Section: Introductionmentioning

confidence: 99%

Phosphodiesterase-Iα/autotaxin's MORFO domain regulates oligodendroglial process network formation and focal adhesion organization

Dennis

White

Forrest

et al. 2008

Molecular and Cellular Neuroscience

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Development of a complex process network by maturing oligodendrocytes is a critical but currently poorly characterized step toward myelination. Here, we demonstrate that the matricellular oligodendrocyte-derived protein phosphodiesterase-Iα/autotaxin (PD-Iα/ATX) and especially its MORFO domain are able to promote this developmental step. In particular, the single EF hand-like motif located within PD-Iα/ATX's MORFO domain was found to stimulate the outgrowth of higher order branches but not process elongation. This motif was also observed to be critical for the stimulatory effect of PD-Iα/ATX's MORFO domain on the reorganization of focal adhesions located at the leading edge of oligodendroglial protrusions. Collectively, our data suggest that PD-Iα/ATX promotes oligodendroglial process network formation and expansion via the cooperative action of multiple functional sites located within the MORFO domain and more specifically, a novel signaling pathway mediated by the single EF hand-like motif and regulating the correlated events of process outgrowth and focal adhesion organization.

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Section: Introductionmentioning

confidence: 99%

Phosphodiesterase-Iα/autotaxin's MORFO domain regulates oligodendroglial process network formation and focal adhesion organization

Dennis

White

Forrest

et al. 2008

Molecular and Cellular Neuroscience

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“…Other BTB-kelch proteins are implicated in cytoskeletal organization. These include Mayven, a brain-specific protein that binds actin and contributes to oligodendrocyte process extensions [7]; Klhdc2, a ubiquitously expressed protein that may be involved with cytoskeletal remodeling in myoblasts [8]; and Nd1-L, which is found in all tissues and appears to stabilize actin filaments [9].…”

Section: Introductionmentioning

confidence: 99%

Krp1 (Sarcosin) promotes lateral fusion of myofibril assembly intermediates in cultured mouse cardiomyocytes

Greenberg

Connelly

Daniels

et al. 2008

Experimental Cell Research

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Krp1, also called sarcosin, is a cardiac and skeletal muscle kelch-repeat protein hypothesized to promote the assembly of myofibrils, the contractile organelles of striated muscles, through interaction with N-RAP and actin. To elucidate its role, endogenous Krp1 was studied in primary embryonic mouse cardiomyocytes. While immunofluorescence showed punctate Krp1 distribution throughout the cell, detergent extraction revealed a significant pool of Krp1 associated with cytoskeletal elements. Reduction of Krp1 expression with siRNA resulted in specific inhibition of myofibril accumulation with no effect on cell spreading. Immunostaining analysis and electron microscopy revealed that cardiomyocytes lacking Krp1 contained sarcomeric proteins with longitudinal periodicities similar to mature myofibrils, but fibrils remained thin and separated. These thin myofibrils were degraded by a scission mechanism distinct from the myofibril disassembly pathway observed during cell division in the developing heart. The data are consistent with a model in which Krp1 promotes lateral fusion of adjacent thin fibrils into mature, wide myofibrils and contribute insight into mechanisms of myofibrillogenesis and disassembly.

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“…MRP2 is involved in glycogen synthase kinase 3␤-mediated neuronal differentiation (24) and process elongation in oligodendrocytes (25,31). MAYVEN is also essential for FYN-modulated process elongation in oligodendrocytes (25). Whereas KEAP1, MRP2, and MAYVEN are endogenously localized in the cytoplasm (8,24,25), NRP/B is endogenously localized in the nucleus (19,32).…”

Section: Expression Of Nrp/b In Neuronal Cells-nrp/b Has Beenmentioning

confidence: 99%

“…KEAP1, another Kelch family member, functions as transcriptional repressor for NRF2 (8), whereas NRP/B is an enhancer for NRF2 activity (17,20). MRP2 is involved in glycogen synthase kinase 3␤-mediated neuronal differentiation (24) and process elongation in oligodendrocytes (25,31). MAYVEN is also essential for FYN-modulated process elongation in oligodendrocytes (25).…”

Section: Expression Of Nrp/b In Neuronal Cells-nrp/b Has Beenmentioning

confidence: 99%

“…MAYVEN is also essential for FYN-modulated process elongation in oligodendrocytes (25). Whereas KEAP1, MRP2, and MAYVEN are endogenously localized in the cytoplasm (8,24,25), NRP/B is endogenously localized in the nucleus (19,32). We examined the differential effects of these proteins on NRF2-mediated HO1 transcriptional activity using a luciferase reporter assay.…”

Section: Expression Of Nrp/b In Neuronal Cells-nrp/b Has Beenmentioning

confidence: 99%

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Nuclear Matrix Protein (NRP/B) Modulates the Nuclear Factor (Erythroid-derived 2)-related 2 (NRF2)-dependent Oxidative Stress Response

Seng

Avraham

Birrane

et al. 2010

Journal of Biological Chemistry

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Reactive molecules have diverse effects on cells and contribute to several pathological conditions. Cells have evolved complex protective systems to neutralize these molecules and restore redox homeostasis. Previously, we showed that association of nuclear factor (NF)-erythroid-derived 2 (E2)-related factor 2 (NRF2) with the nuclear matrix protein NRP/B was essential for the transcriptional activity of NRF2 target genes in tumor cells. The present study demonstrates the molecular mechanism by which NRP/B, via NRF2, modulates the transcriptional activity of antioxidant response element ( Mammalian cells are exposed to reactive molecules originating from several exogenous and endogenous sources (1, 2). These molecules include reactive oxygen species, electrophilic chemicals, and heavy metals, which induce oxidative stress that impairs cellular functions and results in diverse pathological conditions, such as cancer, cardiovascular disease, diabetes, and neurodegenerative disorders (2-5). In response to these reactive molecules, cells have evolved multiple protective mechanisms to neutralize and clear toxic molecules and restore cellular redox homeostasis. One of these mechanisms is modulated by the nuclear factor (NF) 2 -E2-related factor 2 (NRF2) protein (6), which binds to ARE promoter sequences, leading to the coordinated up-regulation of ARE-driven detoxifying and antioxidant genes (7-11). The NRF2 system confers a protective effect on mammalian cells from a variety of toxic insults including carcinogens, reactive oxygen species, diesel exhaust, inflammation, calcium disturbance, UV light, and cigarette smoke (6).Kelch-related proteins contain an N-terminal BTB (Broadcomplex, Tramtrack, Bric-a-brac) domain that is primarily found in zinc finger proteins and functions as a homo-or heterodimerization domain (12, 13) and a C-terminal Kelch repeat or ␤-propeller domain that binds actin tails and has important roles in protein folding and as a protein-protein interaction module (12, 13). Multiprotein complexes formed through contact sites in ␤-propeller domains (14) are believed to be important for gene expression, cytoskeletal maintenance (15, 16), and controlling cellular organization and morphology (15, 16). Importantly, alterations or mutations in Kelch-related proteins have been found in numerous tumors (14, 17) and neurodegenerative disorders (18). The cytoplasmic protein Kelch-like ECH-associated protein 1 (KEAP1) and the nuclear NRP/B are both members of the Kelch-related family (8,19). The localization of these proteins is important for regulation of the NRF2 pathway in which KEAP1 and NRP/B/ENC1 suppress and enhance, respectively, NRF2-mediated phase II detoxifying and antioxidant enzymes in response to oxidative stress (8,17,20).Six functional domains of NRF2, termed NRF2 ECH homology (Neh) 1-6, have been identified and found to be highly conserved in various species (8). Neh1 is a bZip motif that mediates DNA binding and participates in heterodimerization with 2 The abbreviations used are: NF, nuclear f...

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Process elongation of oligodendrocytes is promoted by the Kelch‐related actin‐binding protein Mayven

Cited by 30 publications

References 46 publications

Phosphodiesterase-Iα/autotaxin's MORFO domain regulates oligodendroglial process network formation and focal adhesion organization

Phosphodiesterase-Iα/autotaxin's MORFO domain regulates oligodendroglial process network formation and focal adhesion organization

Krp1 (Sarcosin) promotes lateral fusion of myofibril assembly intermediates in cultured mouse cardiomyocytes

Nuclear Matrix Protein (NRP/B) Modulates the Nuclear Factor (Erythroid-derived 2)-related 2 (NRF2)-dependent Oxidative Stress Response

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