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1

Miozyny a patologia

100%
Redowicz M. J.
Kosmos
|
2001
|
tom 50
|
nr 3
315-324
2

Miozyny niekonwencjonalne - budowa a potencjalne funkcje w komorce

100%
Redowicz M. J.
Kosmos
|
2001
|
tom 50
|
nr 4
375-390
3

Limb girdle muscle dystrophies: genetic, clinical, and biochemical diversity in Polish patients

100%
Redowicz M. J.
Acta Biologica Cracoviensia. Series Botanica. Supplement
|
2016
|
tom 58
|
nr 1
4

Role of Myosin VI-DOCK7 interaction in neuronal cells

100%
Redowicz M. J.
Acta Neurobiologiae Experimentalis
|
2017
|
tom 77
|
nr Suppl.1
Myosin VI (MVI) is a unique unconventional myosin as unlike all other myosins it walks towards the minus (pointed) end of actin filaments. It is involved in many cellular functions related to intracellular transport and organization of the actin cytoskeleton. MVI involvement in a given function depends on its interactions with its tissue/cell specific partners. Several studies show that MVI plays a role in glutamate receptor internalization, synaptic transmission and synaptic vesicle recycling. Our search for MVI partners resulted in identification of DOCK7 as its potential partner in neuronal-lineage PC12 cells. Since DOCK7, a protein with GEF activity towards Rac1 and Cdc42, is crucial for axon formation, we aimed at characterization of physiological relevance of this novel interaction in neuronal cells, including neurosecretory PC12 cells and primary culture neurons. We confirmed that this interaction occurred also in neurons, and biochemically characterized MVI-DOCK7 binding sites. The presence of MVI was necessary for both DOCK7 localization and activity as well as for NGF-stimulated protrusion formation, as revealed for PC12 cells. Studies on primary culture neurons revealed that co-localization of both proteins was maintained during the culture time-course and was visible within cell body, neurites, dendritic spines and neurite growth cones. Also, lack or depletion of MVI affected the dendritic arbor formation and morphology of axonal growth cone. MVI-DOCK7 co-localization was also visible in the brain. Studies on brains of Snell’s waltzer mice (SV) that do not synthesize MVI also revealed a decrease of DOCK7 activity measured by the levels its own and its downstream effectors phosphorylation. Of note, SV mice exhibit several neuronal dysfunctions such as deafness, circling and head tossing behavior. Taken together, our data indicate that MVI-DOCK7 interaction plays important role in the neuronal system. FINANCIAL SUPPORT: The work was supported by a grant UMO-2012/05/B/NZ3/01996 from the National Science Centre and statutory funds for the Nencki Institute of Experimental Biology from Ministry of Science and Higher Education.
5

Myosins and pathology: genetics and biology

100%
Redowicz M. J.
Acta Biochimica Polonica
|
2002
|
tom 49
|
nr 4
This article summarizes current knowledge on the genetics and possible molecular mechanisms of human pathologies resulted from mutations within the genes encoding several myosin isoforms. Mutations within the genes encoding some myosin isoforms have been found to be responsible for blindness (myosins III and VIIA), deafness (myosins I, IIA, IIIA, VI, VIIA and XV) and familial hypertrophic cardiomyopathy (β cardiac myosin heavy chain and both the regulatory and essential light chains). Myosin III localizes predominantly to photoreceptor cells and is proved to be en­gaged in the vision process in Drosophila. In the inner ear, myosin I is postulated to play a role as an adaptive motor in the tip links of stereocilia of hair cells, myosin IIA seems to be responsible for stabilizing the contacts between adjacent inner ear hair cells, myosin VI plays a role as an intracellular motor transporting membrane structures within the hair cells while myo- sin VIIA most probably participates in forming links between neighbouring stereocilia and myosin XV probably stabilizes the stereocilia structure. About 30% of patients with familial hypertrophic cardiomyopathy have mutations within the genes encoding the β cardiac myosin heavy chain and both light chains that are grouped within the regions of myosin head crucial for its functions. The alter­ations lead to the destabilization of sarcomeres and to a decrease of the myosin ATPase activity and its ability to move actin filaments.
6

Pierwotniaki w badaniach biochemicznych i genetycznych

88%
Redowicz M. J.
Kosmos
|
2000
|
tom 49
|
nr 4
583-587
7

Nonmuscle myosins in muscle pathologies

88%
Redowicz M. J.
Acta Neurobiologiae Experimentalis
|
2007
|
tom 67
|
nr 3
8

Role of unconventional Myosin VI in localization and activity of DOCK7 in the brain

63%
Chumak V., Redowicz M. J.
Acta Neurobiologiae Experimentalis
|
2017
|
tom 77
|
nr Suppl.1
INTRODUCTION: Myosin VI (MVI) is a unique unconventional motor that moves toward the minus end of actin filaments. It is involved in endocytosis, cellular trafficking, cell migration and adhesion. The spontaneous mutation of a mouse Myo6 gene resulted in a characteristic circling phenotype (termed as Snell’s waltzer, SV) with sensorineural deafness and neurological symptoms accompanied by abnormalities in other organs. DOCK7 (dedicator of cytokinesis 7), a guanidine nucleotide exchange factor (GEF) for Rac1 and Cdc42 GTP that plays a role in axon formation and neuronal polarization, is a binding partner of MVI. We also characterized the MVI-DOCK7 interaction sites and showed that in PC12 cells the interaction was important for DOCK7 activity and NGF-stimulated protrusion formation. AIM(S): The main aim of this work is elucidation of the role of MVI in brain development and function. METHOD(S): Western-blot, confocal microscopy RESULTS: In hippocampus of WT brains, DOCK7 colocalized with MVI mainly in the perinuclear region. In the SV brains, DOCK7 distribution was more diffusive, not resembling the puncti‑like defined structures visible in the WT samples. Also, the absence of MVI affected DOCK7 activity asrevealed by estimation of the levels of phosphorylated (active) forms of DOCK7 and its downstream effector SAPK/JNK kinase. Moreover, a significantincrease ofthe levels of GFAP (glial fibrillary acidic protein) and caspase-3 were observed in the in hippocampus and cerebral cortex of SV brains. CONCLUSIONS: MVI is important both for DOCK7 distribution and activity, and that this interaction could play important role(s) in neuronal functions.
9

Is Amoeba proteus myosin VI immunoanalogue a dimeric protein?

63%
Sobczak M., Redowicz M. J.
Acta Protozoologica
|
2005
|
tom 44
|
nr 4
10

Effects of blocking of endogenous Rho family GTP-binding proteins on morphology, adhesion and locomotion of Amoeba proteus

63%
Klopocka W., Redowicz M. J.
Cellular and Molecular Biology Letters
|
2001
|
tom 06
|
nr 2
11

Detection of Rho-family proteins in Acanthamoeba castellanii

63%
Redowicz M. J., Korn E. D.
Acta Protozoologica
|
2000
|
tom 39
|
nr 1
12

Non-muscle myosins in muscle

63%
Redowicz M. J.
Acta Biochimica Polonica
|
2006
|
tom 53
|
nr Supplement 1
13

Miozyny w jądrze komórkowym

51%
Sobczak M., Majewski L., Redowicz M. J.
Postępy Biochemii
|
2009
|
tom 55
|
nr 2
14

Myosin VI in mouse spermatogenesis

51%
Zakrzewski P., Lenartowski R., Redowicz M. J., Lenartowska M.
Acta Biologica Cracoviensia. Series Botanica. Supplement
|
2016
|
tom 58
|
nr 1
15

Myosin VI is associated with secretory granules and is present in the nucleus in adrenal medulla chromaffin cells

51%
Majewski L., Sobczak M., Redowicz M. J.
Acta Biochimica Polonica
|
2010
|
tom 57
|
nr 1
109-114
Myosin VI (MVI) is the only known myosin walking towards minus end of actin filaments. Here, MVI, but not myosins IB or IIB, was detected in chromaffin granules isolated from bovine medulla and found to be tightly associated with the granule apical surface. MVI also localized to secretory granules within rat pheochromocytoma PC12 cells as well as to the Golgi apparatus, endoplasmic reticulum and clathrin-coated pits. Notably, it was also found in the nucleus. RT-PCR revealed that MVI splice variants with a large insert (LI), characteristic of polarized cells, were barely detectable in PC12 cells, whereas variants with a small insert (SI) were the major isoforms. The presented data indicate that MVI in adrenal medulla cells is engaged in secretory vesicle trafficking within the cytoplasm and possibly also involved in transport within the nucleus.
16
Content available remote

The content of myosin heavy chains in hindlimb muscles of female and male rats

51%
Drzymala-Celichowska H., Karolczak J., Redowicz M. J., Bukowska D.
Journal of Physiology and Pharmacology
|
2012
|
tom 63
|
nr 2
17

Regulacja dynamiki cytoszkieletu kortykalnego podczas migracji swobodnie żyjacych ameb

51%
Klopocka W., Redowicz M. J., Wasik A.
Postępy Biochemii
|
2009
|
tom 55
|
nr 2
18

Response of Amoeba proteus to microinjection with active Rac1 and RhoA proteins

51%
Pawlowska M., Pomorski P., Klopocka W., Redowicz M. J.
Acta Protozoologica
|
2003
|
tom 42
|
nr 3
19

Codon usage in Amoeba proteus significantly differs from Entamoeba histolytica and Acanthamoeba castellanii

51%
Kocik E., Sobczak M., Redowicz M. J.
Acta Protozoologica
|
2006
|
tom 45
|
nr 3
20

Role of Amot12, Rast8 and Homer1 in the organization of postsynaptic machinery

39%
Gawor M., Niewiadomski P., Bernadzki K., Jozwiak J., Rojek K., Redowicz M. J., Proswzynski T. J.
Acta Neurobiologiae Experimentalis
|
2015
|
tom 75
|
nr Supl.
BACKGROUND AND AIMS: Vertebrate neuromuscular junction (NMJ) undergoes a series of topological rearrangements in order to achieve its mature complex shape resembling pretzels. We have previously reported that podosomes, actin-rich dynamic adhesive organelles are implicated in the NMJ developmental remodeling. The main aim of this study was to understand molecular mechanisms regulating formation of podosomes and/or remodeling of the postsynaptic machinery with a special focus on the role of Amotl2 scaffold protein in these processes. METHODS: To identify Amotl2-binding proteins we used TAP-tag affinity purification and mass spectrometry. Localization of proteins to NMJ subsynaptic compartments was performed using standard cytochemical procedures and confocal microscopy. We performed RNAi-based knockdown experiments on cultured C21C12 myotubes to assess the importance of proteins in the organization of postsynaptic AChR clusters. RESULTS: We identified several novel Amotl2-binding proteins and subsequently focused our experiments on two of them, Rassf8 and Homer1, that remain uncharacterized at the NMJ. Amotl2, Rassf8 and Homer1 are concentrated at postsynaptic areas of NMJs in the indentations between the AChR-rich branches. Our results suggest that Rassf8 and Homer1 may be involved in AChR organization and development of the neuromuscular synapses. CONCLUSIONS: We identified novel components of the muscle postsynaptic machinery that specifically localize to the sites of NMJ remodeling. Our results suggest that Amotl2 may be involved in the developmental remodeling of the postsynaptic machinery through the interactions with Rassf8 and Homer1. This research was supported by the NCN grant 2012/05/E/ NZ3/00487.
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