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Ridley A., Clark P., Peckham M. — Cell motility: from molecules to organisms
Ridley A., Clark P., Peckham M. — Cell motility: from molecules to organisms



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Название: Cell motility: from molecules to organisms

Авторы: Ridley A., Clark P., Peckham M.

Аннотация:

Recent advances in molecular and biophysical techniques, particularly fluorescence and live cell imaging, are revolutionizing the study of cell motility. New bioprobes not only reveal simple intracellular localization, but also contain details of post-translational modifications, conformational state and protein-protein interactions. Coupling these insights with complementary advances in genetic and biochemical methods is enabling scientists to understand the processes involved in cell motility - from molecular motors to cell movements in vivo in a range of organisms and cell types.

This book features landmark essays that provide an up to date and fascinating account of current research and concepts in cell motility.These cover the roles of molecular motors that drive movement and their interactions with the cytoskeleton as well as membrane dynamics that allow cells to change shape and to move.

Cell motility plays a key role in development - there are chapters on the genetics of cell migration, the regulation of contact repulsion in growth cones, and the progression from cell migration to cell-cell adhesion. Cell motility is directional - experts describe the molecules that regulate chemotaxis, allowing cells to migrate along pathways specified by chemical gradients. Finally, cell motility can be perturbed by mutation—metastasis occurs when cells lose their normal intercellular interactions and invade other tissue types. All these processes are regulated by signals from the environment, including other tissues in the body, and the various molecules that transmit and transduce these signals are discussed.

This book is a ‘must read’ for cell biologists working in a variety of fields, from development to wound healing, at all levels - post-doctoral fellows, post-graduate students and lab technicians. It is also stimulating reading for molecular and developmental biologists, biophysicists and biochemists.


Язык: en

Рубрика: Биология/

Статус предметного указателя: Готов указатель с номерами страниц

ed2k: ed2k stats

Год издания: 2004

Количество страниц: 342

Добавлена в каталог: 10.12.2005

Операции: Положить на полку | Скопировать ссылку для форума | Скопировать ID
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Предметный указатель
LIS1      88 90
Listeria      146 156
Listeria monocytogenes      137—138 143 145
Local cell intercalation rates and tissue-level displacement      288
m-calpain (calpain II)      223
M10      26
M10, relationship to DdM7      31—32
M7      26
M7, link with talin      28—30
M7a      27
MAP      87
MAP kinase cascades      269
Matrix adhesions      78
Matrix metalloproteases (MMPs)      160—161
MDCK cells      54 101 104 108 160 239—240 242
MDCK cells in cell-cell adhesion      105
MDCK cells, cadherin-dependent cell-cell adhesion in      107
MDCK cells, Racl complexes in, during cell-cell adhesion      109
MDCK cells, Racl-containing lamellipodia drive cell-cell contact formation between      107
MDCK cells, RacT17NGFP in      109
mDia, activation by active RhoA      84
mDial      75 78 83 85 144
mDial activity      90
mDial as coordinator of actin, focal adhesions and microtubule assembly      84—91
mDial, cytoskeletal alterations produced by      86
mDial, effects on microtubule dynamics      87
mDial, role in organization of microtubule system      91
mDial-induced changes in microtubule dynamics      92
mDial-mediated microtubule regulation      87
Mediolateral cell intercalation      277
Mediolateral intercalation      279—280 284
MEK kinase signalling, chemotaxis regulated by      269—271
MEK1      261
Melanoma B16 cells      79
Melb-a melanoblasts      79
Membrane domains      102
Membrane dynamics      165—171
Membrane dynamics in cell-cell adhesion      106—107
Membrane protrusion      170
Membrane recycling      169
Membrane translocation      167
Mesodermal cells      293
Mesodermal tissues      289
Metastatic cells, chemotaxis      175
Metazoan cell types      203
Metazoans, morphogenesis of      277
Microtubule cytoskeleton      203
Microtubule cytoskeleton, organization and dynamics of      208
Microtubule dynamics      206
Microtubule dynamics in migrating cells      203—217
Microtubule dynamics, instability downstream of Rac1      210—213
Microtubule dynamics, mDial-induced changes in      92
Microtubule organization      203 206
Microtubule plus ends      206
Microtubule stabilization, downstream of RhoA      209—210
Microtubule stabilization, mDia-mediated      209
Microtubule-disrupting drugs      78
Microtubule-end-tracking proteins      90
Microtubule-mediated suppression of contractility      81
microtubules      75—99
Microtubules, disruption of      81
Microtubules, role in migrating cells      80 205—207
Microvilli      236
Mitogen-activated protein kinase (MAPK)      226
ML-7      81
Morphogenesis      277
Morphogenic processes      277
Mouse development, cell migration during      317—330
MTC cells, EGF receptor in      177
MTLn3      176—179
Multicellular organisms      101
Muscle precursor cells      325—328
Muscle precursor cells, development of      324
Muscle precursor cells, Eph receptor signals during migration of      328
Myo1c      54
Myo3p      49—50
Myo5p      49—51
MyoA      44 49
MYOB      44 49 51
MyoC      44 51
MyoD      44
MyoE      44
MyoF      44
Myogenic precursor cells      326
MyoK      44—48 51
MyoK GPR loop      47
MyoK, molecular functions      52
Myosin ATPase (BDM)      81
Myosin I      39—59
Myosin I and actin dynamics connection      49—52
Myosin I, phenotypes resulting from manipulation      48—49
Myosin IB      44
Myosin IC      44
Myosin IE      44—45
Myosin IF      44
Myosin II      42 81—83 136 226 262—263
Myosin II-driven cell contractility      75
Myosin II-driven contractility      80—81 92
Myosin light chain phosphatase (MLCP)      92
Myosin superfamily      40—42
Myosin VII, role in adhesion      19—37
Myosin X      123
Myosins, structure function analysis      44—48
Myotome (MY)      326
MyTH4/FERM module      31
N-CAM      310—311
N-WASp      9 138 141 155 161 247—260
N-WASp in podosome formation and tubulogenesis      159—160
N-WASp, mechanism of activation      157—159
N17Rac      66
Nap124      141
Nap125      159
Nck      64
Nck Associated protein 1 (NCKAP1)      251
NDF (Neu Differentiation Factor)      319
Neural cells      281
Neural cells, intercalation      282
Neural crest cells      320
Neural crest cells, development of      321—323
Neural crest cells, migration of      318 320—321
Neuronal axons      71
Neuronal precursors in rostral migratory stream (RMS)      310—312
Neurulation      277—279
Neutrophil chemotaxis, calpain in regulating      229
Nrg1      318—321
Nucleation-promoting factors      7—8
Nucleotide hydrolysis      9
Opl8/stafhmin      90 206
Opl8/stafhmin, phosphorylation of      211
P13K1/2      267
p41-Arc      137
p85-PI3 kinase      64
Pak      11 50 303 309
PAK kinase      40
PAK/LIM kinase pathway      13
PAK/Ste20 family      41
PAK1      208
PAK1-mediated phosphorylation      90
Paraxial protocadherin (PAPC)      292
Paxillin      299 301 303—304 306 309
Paxillin adhesions      303
PDGF      193
PDGF-dependent activation of tyrosine kinase      120
PDZ      27
pECFP-C1      128
pEYFP-C1      128
PH domain      111 167—168 190 198
PH domain localization, mechanisms controlling      263—265
PH domain translocation kinetics      268
PH domain translocation to leading edge      271
Phagocytosis      170
Phalloidin      9
phg1      23—24
Phosphatidic acid (PA)      170
Phosphatidylinositol (4)-phosphate 5-kinase (PIP 5K)      170
Phosphatidylinositol (4,5)-bis-phosphate ($PIP_{2}$)      125 136 170
Phosphatidylinositol 3-kinase      see “PI3K”
Phosphoinositide (PI) lipids      190
Phosphoinositide 3-kinase      see “PI3K”
Phosphoinositide 3’-phosphatase      see “PTEN”
Phosphoinositides (D3-PI)      261
Phospholipase D (PLD)      170—171
Phospholipase P (PLC)      181 238
Photoactivation of fluorescence (PAF)      127
PI3K      31 111 167 179—180 182 185 261 263
PI3K in chemotaxis      263—265
PI3K, activation      168
PI3K, translocates upon stimulation with chemoattractant      265—267
PI3K, translocation kinetics      268
PI3K1, constitutive localization      266
PIP5K      171
PIP5KI      190
PIR121      141 158—159 251
PIX      303 309
pKa      225
Plasma membranes      103 183 193 300
Pleckstrin homology      see “PH”
Podosomes, formation of      159—160
Polymerization-depolymerization transition      207
Polyphosphoinositides      136
Polysialic acid chains (PSA)      310—311
Postsynaptic density (PSD)      197
Pre-bleach images, FLAP      130
Pro      45
Profilin      1 3—4 40
Proline-arginine-rich domain (PRD)      47 50 190 192 195 198
Protein dynamics      117-134
Protein kinase $C\alpha$ ($PKC\alpha$)      122
Protein kinase P (PKC)      185 222—223
Protocadherins      292
Protrusion      300
Pseudopod formation      170
PTEN      180 261 264 271
PTEN as negative regulator of D3-PI signalling pathway in chemotaxis      267—269
PTEN, translocation kinetics      268
PTEN-GFP      269
PtK1      206 210—212
RAc      65—67 154 241 310
Rac GTPase      120
Rac-mediated Rho activation      67
Rac1      107 112 203 205 208—209
Rac1, localization and activity      108
Rac1, microtubule dynamic instability downstream of      210—213
Rac1, mutant expression effects on endogenous Rac1 complexes and cell behaviour      108
Rac1-containing lamellipodia drive cell-cell contact formation between MDCK cells      107
Rac1-driven process      106
Rac1:PAK effector complex      108
Rac1G12V      110
Rac1Q61L      110
Rac1T17N      110
RacGFP localization      107
RacGFP localization, changes in      108
RacGFP, accumulation of      107
Racl complexes      111
Racl complexes and cell-cell contact      108
Racl complexes in MDCK cells during cell-cell adhesion      109
Racl complexes, linking back to mechanisms of cell cell adhesion      111—112
RacT17NGFP in MDCK cells      109
Radial intercalation      284
Receptor tyrosine kinases      7
Receptor-mediated endocytic (RME) machinery      194
Restriction enzyme mediated insertion (REMI) mutagenesis      44
Retinal ganglion cells (RGCs)      63 71
Retinal ganglion cells (RGCs), axons      63 67
Retinal ganglion cells (RGCs), ephrin-induced growth cone collapse in      67
Retinal ganglion cells (RGCs), growth cones      61 63 69—70
Retrograde-flow-induced breakage      208
Rho      65 75 83
Rho activation, Rac-mediated      67
Rho associated kinase (ROCK)      67 69 71 75 83 87 92
Rho GTPases      12 40 61 76 78 120 203—217 248 257
Rho GTPases as molecular switches      204
Rho GTPases in cell-cell adhesion      106—107
Rho GTPases, activation      106
Rho GTPases, role in ephrin induced growth cone collapse      67—71
Rho-binding domain (RBD)      84
Rho-family members      170
Rho-Rho kinase pathway      68
Rho/Rac/Cdc42 family      41
RhoA      154 203 209
RhoA, microtubule stabilization downstream of      209—210
Robo      7
Rostral migratory stream (RMS)      299 309
Rostral migratory stream (RMS), cell migration of neuronal precursors in      310—311
Rostral migratory stream (RMS), neuronal precursors in      312
Saccharomyces      250
Saccharomyces cerevisiae      40 44 50 137 167 255
SadA      24
Scanning confocal fluorescence microscopy      290
Scanning electron micrography      290
Scar      8 249—260
Scar, regulation of      250—251
Scar/WAVE      140
Scar1      139 254
Scar1, discovery of      253
Scar1/WAVE1      141
SCAR1—3      138
Scatter factor/hepatocyte growth factor (SF/HGF)      324
Schizosaccharomyces pombe      44 50 137
Schwann cell precursors      321
Sec7 domains      167
Semaphorin3A      67
SF/HGF      324—327
SH3      45 49 192
Shigella      156
Shigella flexneri      235 239
SHP2      325
Signalling pathways      6—8 71 185 255 267—269
Single cell imaging      121
Slice technology      313
Slit      7
Soluble ephrin      70
Soluble ephrin, Eph receptor activation by      65
Soluble ephrin-A5      71
Somitic migration      310
SOP2Hs      137
Sox10      321
Spatio-temporal signalling relationships      121
SRC      64 222—223
Src homology 3 (SH3)      190
Subcellular targeting of GPCR downstream effectors during chemotaxis      261—275
Subventricular zone (SVZ)      310
sumo      270—271
SUMOylation      270—271
Supervillin      236 238
Surface receptors      19
Swiss 3T3 cells      65
Swiss 3T3 fibroblasts      61 70 125
T cells      207
Tail homology (TH) domains      44
TalA      25 28—29
Talin, link with M7      28—30
Talin, role in adhesion      19—37
TalinA      24—26
TalinB      25—26
Taricha torosus      279
TEDS      40 42 50 52
Tfn-R      168
TH1      42 44—45 48
TH2      42 45 48
1 2 3 4
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