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DICDI:MYS2

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Species (Taxon ID) Dictyostelium discoideum (Slime mold). (44689)
Gene Name(s) mhcA
Protein Name(s) Myosin-2 heavy chain

Myosin II heavy chain

External Links
UniProt P08799
EMBL M14628
AAFI02000085
PIR A26655
RefSeq XP_637740.1
PDB 1D0X
1D0Y
1D0Z
1D1A
1D1B
1D1C
1FMV
1FMW
1G8X
1JWY
1JX2
1LVK
1MMA
1MMD
1MMG
1MMN
1MND
1MNE
1Q5G
1VOM
1W9I
1W9J
1W9K
1W9L
1YV3
2AKA
2JHR
2JJ9
2X9H
2XEL
2XO8
2Y0R
2Y8I
2Y9E
3BZ7
3BZ8
3BZ9
3MJX
3MKD
3MNQ
3MYH
3MYK
3MYL
4AE3
PDBsum 1D0X
1D0Y
1D0Z
1D1A
1D1B
1D1C
1FMV
1FMW
1G8X
1JWY
1JX2
1LVK
1MMA
1MMD
1MMG
1MMN
1MND
1MNE
1Q5G
1VOM
1W9I
1W9J
1W9K
1W9L
1YV3
2AKA
2JHR
2JJ9
2X9H
2XEL
2XO8
2Y0R
2Y8I
2Y9E
3BZ7
3BZ8
3BZ9
3MJX
3MKD
3MNQ
3MYH
3MYK
3MYL
4AE3
ProteinModelPortal P08799
SMR P08799
DIP DIP-46078N
IntAct P08799
STRING 44689.DDB_0191444
PRIDE P08799
EnsemblProtists DDB0191444
GeneID 8625606
KEGG ddi:DDB_G0286355
dictyBase DDB_G0286355
eggNOG COG5022
InParanoid P08799
KO K10352
OMA EHINREN
PhylomeDB P08799
EvolutionaryTrace P08799
Proteomes UP000002195
UP000002195
GO GO:0042641
GO:0005826
GO:0045179
GO:0005938
GO:0031254
GO:0005856
GO:0005829
GO:0032009
GO:0032982
GO:0016460
GO:0097204
GO:0001931
GO:0071889
GO:0051015
GO:0030898
GO:0030554
GO:0005524
GO:0000146
GO:0003774
GO:0042803
GO:0033275
GO:0006200
GO:0032060
GO:0006928
GO:0006935
GO:0030038
GO:0033298
GO:0030866
GO:0031154
GO:0060328
GO:0046847
GO:0006971
GO:0008152
GO:0000281
GO:0031034
GO:0030837
GO:0008104
GO:0031270
GO:0042542
GO:0034461
Gene3D 4.10.270.10
InterPro IPR000048
IPR027401
IPR001609
IPR004009
IPR008989
IPR002928
IPR027417
Pfam PF00063
PF02736
PF01576
PRINTS PR00193
SMART SM00015
SM00242
SUPFAM SSF50084
SSF52540
PROSITE PS50096
PS51456

Annotations

Qualifier GO ID GO term name Reference ECO ID ECO term name with/from Aspect Extension Notes Status

part_of

GO:0031012

extracellular matrix

PMID:26152465[1]

ECO:0007005

high throughput direct assay evidence used in manual assertion

C

part_of:(GO:0031153)

Seeded From UniProt

complete

involved_in

GO:0051591

response to cAMP

PMID:2543508[2]

ECO:0000314

direct assay evidence used in manual assertion

P

Seeded From UniProt

complete

acts_upstream_of_or_within

GO:0050982

detection of mechanical stimulus

PMID:22379107[3]

ECO:0000315

mutant phenotype evidence used in manual assertion

P

Seeded From UniProt

complete

part_of

GO:0031410

cytoplasmic vesicle

PMID:3243031[4]

ECO:0000314

direct assay evidence used in manual assertion

C

Seeded From UniProt

complete

part_of

GO:0030864

cortical actin cytoskeleton

PMID:3243031[4]

ECO:0000314

direct assay evidence used in manual assertion

C

Seeded From UniProt

complete

colocalizes_with

GO:0032154

cleavage furrow

PMID:19515202[5]

ECO:0000314

direct assay evidence used in manual assertion

C

Seeded From UniProt

complete

acts_upstream_of_or_within

GO:0008360

regulation of cell shape

PMID:8874966[6]

ECO:0000315

mutant phenotype evidence used in manual assertion

P

Seeded From UniProt

complete

acts_upstream_of_or_within

GO:0031152

aggregation involved in sorocarp development

PMID:25887420[7]

ECO:0000270

expression pattern evidence used in manual assertion

P

Seeded From UniProt

complete

part_of

GO:0005829

cytosol

PMID:23132928[8]

ECO:0000314

direct assay evidence used in manual assertion

C

exists_during:(GO:0051593)

Seeded From UniProt

complete

part_of

GO:1990753

equatorial cell cortex

PMID:19515202[5]

ECO:0000314

direct assay evidence used in manual assertion

C

Seeded From UniProt

complete

acts_upstream_of_or_within

GO:0009612

response to mechanical stimulus

PMID:23442953[9]

ECO:0000315

mutant phenotype evidence used in manual assertion

P

Seeded From UniProt

complete

involved_in

GO:0042542

response to hydrogen peroxide

PMID:21988699[10]

ECO:0000314

direct assay evidence used in manual assertion

P

Seeded From UniProt

complete

involved_in

GO:1903013

response to differentiation-inducing factor 1

PMID:25518940[11]

ECO:0007005

high throughput direct assay evidence used in manual assertion

P

Seeded From UniProt

complete

part_of

GO:0097204

phagocytic cup base

PMID:12952073[12]

ECO:0000314

direct assay evidence used in manual assertion

C

Seeded From UniProt

complete

enables

GO:0071889

14-3-3 protein binding

PMID:20951045[13]

ECO:0000353

physical interaction evidence used in manual assertion

UniProtKB:P54632

F

Seeded From UniProt

complete

acts_upstream_of_or_within

GO:0060328

cytoplasmic actin-based contraction involved in forward cell motility

PMID:18388319[14]

ECO:0000315

mutant phenotype evidence used in manual assertion

P

Seeded From UniProt

complete

enables

GO:0051015

actin filament binding

PMID:18067324[15]

ECO:0000314

direct assay evidence used in manual assertion

F

Seeded From UniProt

complete

enables

GO:0051015

actin filament binding

PMID:16982629[16]

ECO:0000314

direct assay evidence used in manual assertion

F

Seeded From UniProt

complete

acts_upstream_of_or_within

GO:0046847

filopodium assembly

PMID:15855234[17]

ECO:0000315

mutant phenotype evidence used in manual assertion

P

Seeded From UniProt

complete

part_of

GO:0045179

apical cortex

PMID:22902739[18]

ECO:0000314

direct assay evidence used in manual assertion

C

Seeded From UniProt

complete

enables

GO:0042803

protein homodimerization activity

PMID:2745547[19]

ECO:0000314

direct assay evidence used in manual assertion

F

Seeded From UniProt

complete

part_of

GO:0042641

actomyosin

PMID:4278009[20]

ECO:0000314

direct assay evidence used in manual assertion

C

Seeded From UniProt

complete

acts_upstream_of_or_within

GO:0034461

uropod retraction

PMID:18388319[14]

ECO:0000315

mutant phenotype evidence used in manual assertion

P

Seeded From UniProt

complete

acts_upstream_of_or_within

GO:0033298

contractile vacuole organization

PMID:19843280[21]

ECO:0000315

mutant phenotype evidence used in manual assertion

P

Seeded From UniProt

complete

involved_in

GO:0033275

actin-myosin filament sliding

PMID:19955408[22]

ECO:0000314

direct assay evidence used in manual assertion

P

Seeded From UniProt

complete

involved_in

GO:0033275

actin-myosin filament sliding

PMID:16901894[23]

ECO:0000314

direct assay evidence used in manual assertion

P

Seeded From UniProt

complete

part_of

GO:0032982

myosin filament

PMID:4278009[20]

ECO:0000314

direct assay evidence used in manual assertion

C

Seeded From UniProt

complete

colocalizes_with

GO:0032154

cleavage furrow

PMID:8552657[24]

ECO:0000314

direct assay evidence used in manual assertion

C

Seeded From UniProt

complete

acts_upstream_of_or_within

GO:0032060

bleb assembly

PMID:16926192[25]

ECO:0000315

mutant phenotype evidence used in manual assertion

P

Seeded From UniProt

complete

acts_upstream_of_or_within

GO:0032060

bleb assembly

PMID:16624291[26]

ECO:0000315

mutant phenotype evidence used in manual assertion

P

Seeded From UniProt

complete

part_of

GO:0032009

early phagosome

PMID:20200225[27]

ECO:0000314

direct assay evidence used in manual assertion

C

Seeded From UniProt

complete

acts_upstream_of_or_within

GO:0031270

pseudopodium retraction

PMID:18388319[14]

ECO:0000315

mutant phenotype evidence used in manual assertion

P

Seeded From UniProt

complete

part_of

GO:0031254

cell trailing edge

PMID:22114350[28]

ECO:0000314

direct assay evidence used in manual assertion

C

Seeded From UniProt

complete

acts_upstream_of_or_within

GO:0031154

culmination involved in sorocarp development

PMID:3576222[29]

ECO:0000315

mutant phenotype evidence used in manual assertion

P

Seeded From UniProt

complete

acts_upstream_of_or_within

GO:0031154

culmination involved in sorocarp development

PMID:2721503[30]

ECO:0000315

mutant phenotype evidence used in manual assertion

P

Seeded From UniProt

complete

colocalizes_with

GO:0031143

pseudopodium

PMID:8552657[24]

ECO:0000314

direct assay evidence used in manual assertion

C

exists_during:(GO:0031270)

Seeded From UniProt

complete

involved_in

GO:0031034

myosin filament assembly

PMID:4278009[20]

ECO:0000314

direct assay evidence used in manual assertion

P

Seeded From UniProt

complete

enables

GO:0030898

actin-dependent ATPase activity

PMID:19955408[22]

ECO:0000314

direct assay evidence used in manual assertion

F

Seeded From UniProt

complete

enables

GO:0030898

actin-dependent ATPase activity

PMID:18067324[15]

ECO:0000314

direct assay evidence used in manual assertion

F

Seeded From UniProt

complete

enables

GO:0030898

actin-dependent ATPase activity

PMID:16982629[16]

ECO:0000314

direct assay evidence used in manual assertion

F

Seeded From UniProt

complete

enables

GO:0030898

actin-dependent ATPase activity

PMID:4278009[20]

ECO:0000314

direct assay evidence used in manual assertion

F

Seeded From UniProt

complete

involved_in

GO:0030866

cortical actin cytoskeleton organization

PMID:16461463[31]

ECO:0000314

direct assay evidence used in manual assertion

P

Seeded From UniProt

complete

acts_upstream_of_or_within

GO:0030837

negative regulation of actin filament polymerization

PMID:15894626[32]

ECO:0000315

mutant phenotype evidence used in manual assertion

P

Seeded From UniProt

complete

enables

GO:0030554

adenyl nucleotide binding

PMID:14620745[33]

ECO:0000314

direct assay evidence used in manual assertion

F

Seeded From UniProt

complete

acts_upstream_of_or_within

GO:0030038

contractile actin filament bundle assembly

PMID:15894626[32]

ECO:0000315

mutant phenotype evidence used in manual assertion

P

Seeded From UniProt

complete

part_of

GO:0016460

myosin II complex

PMID:4278009[20]

ECO:0000314

direct assay evidence used in manual assertion

C

Seeded From UniProt

complete

acts_upstream_of_or_within

GO:0008104

protein localization

PMID:16339076[34]

ECO:0000315

mutant phenotype evidence used in manual assertion

P

Seeded From UniProt

complete

acts_upstream_of_or_within

GO:0006971

hypotonic response

PMID:19843280[21]

ECO:0000315

mutant phenotype evidence used in manual assertion

P

Seeded From UniProt

complete

acts_upstream_of_or_within

GO:0006935

chemotaxis

PMID:16926192[25]

ECO:0000315

mutant phenotype evidence used in manual assertion

P

Seeded From UniProt

complete

acts_upstream_of_or_within

GO:0048870

cell motility

PMID:15259052[35]

ECO:0000316

genetic interaction evidence used in manual assertion

UniProtKB:Q54S20

P

Seeded From UniProt

complete

acts_upstream_of_or_within

GO:0048870

cell motility

PMID:15259052[35]

ECO:0000315

mutant phenotype evidence used in manual assertion

P

Seeded From UniProt

complete

part_of

GO:0005938

cell cortex

PMID:16461463[31]

ECO:0000314

direct assay evidence used in manual assertion

C

Seeded From UniProt

complete

part_of

GO:0005856

cytoskeleton

PMID:2578450[36]

ECO:0000314

direct assay evidence used in manual assertion

C

Seeded From UniProt

complete

part_of

GO:0005826

actomyosin contractile ring

PMID:9238018[37]

ECO:0000314

direct assay evidence used in manual assertion

C

Seeded From UniProt

complete

enables

GO:0005524

ATP binding

PMID:16982629[16]

ECO:0000314

direct assay evidence used in manual assertion

F

Seeded From UniProt

complete

enables

GO:0005524

ATP binding

PMID:4278009[20]

ECO:0000314

direct assay evidence used in manual assertion

F

Seeded From UniProt

complete

enables

GO:0003774

motor activity

PMID:15910751[38]

ECO:0000314

direct assay evidence used in manual assertion

F

Seeded From UniProt

complete

part_of

GO:0001931

uropod

PMID:17126332[39]

ECO:0000314

direct assay evidence used in manual assertion

C

Seeded From UniProt

complete

acts_upstream_of_or_within

GO:0000281

mitotic cytokinesis

PMID:19065153[40]

ECO:0000316

genetic interaction evidence used in manual assertion

UniProtKB:Q54MH2

P

Seeded From UniProt

complete

acts_upstream_of_or_within

GO:0000281

mitotic cytokinesis

PMID:19065153[40]

ECO:0000316

genetic interaction evidence used in manual assertion

UniProtKB:Q8MML5

P

Seeded From UniProt

complete

acts_upstream_of_or_within

GO:0000281

mitotic cytokinesis

PMID:10588668[41]

ECO:0000315

mutant phenotype evidence used in manual assertion

P

Seeded From UniProt

complete

acts_upstream_of_or_within

GO:0000281

mitotic cytokinesis

PMID:3576222[29]

ECO:0000315

mutant phenotype evidence used in manual assertion

P

Seeded From UniProt

complete

acts_upstream_of_or_within

GO:0000281

mitotic cytokinesis

PMID:2721503[30]

ECO:0000315

mutant phenotype evidence used in manual assertion

P

Seeded From UniProt

complete

enables

GO:0000146

microfilament motor activity

PMID:19955408[22]

ECO:0000314

direct assay evidence used in manual assertion

F

Seeded From UniProt

complete

enables

GO:0000146

microfilament motor activity

PMID:16982629[16]

ECO:0000314

direct assay evidence used in manual assertion

F

Seeded From UniProt

complete

enables

GO:0042802

identical protein binding

PMID:15492777[42]

ECO:0000353

physical interaction evidence used in manual assertion

UniProtKB:P08799

F

Seeded From UniProt

complete

enables

GO:0003774

motor activity

GO_REF:0000002

ECO:0000256

match to sequence model evidence used in automatic assertion

InterPro:IPR001609
InterPro:IPR002928
InterPro:IPR004009
InterPro:IPR008989

F

Seeded From UniProt

complete

enables

GO:0005524

ATP binding

GO_REF:0000002

ECO:0000256

match to sequence model evidence used in automatic assertion

InterPro:IPR001609
InterPro:IPR004009
InterPro:IPR008989

F

Seeded From UniProt

complete

part_of

GO:0016459

myosin complex

GO_REF:0000002

ECO:0000256

match to sequence model evidence used in automatic assertion

InterPro:IPR001609
InterPro:IPR002928
InterPro:IPR004009

C

Seeded From UniProt

complete

enables

GO:0051015

actin filament binding

GO_REF:0000002

ECO:0000256

match to sequence model evidence used in automatic assertion

InterPro:IPR008989

F

Seeded From UniProt

complete

part_of

GO:0005737

cytoplasm

GO_REF:0000037

ECO:0000322

imported manually asserted information used in automatic assertion

UniProtKB-KW:KW-0963

C

Seeded From UniProt

complete

enables

GO:0005524

ATP binding

GO_REF:0000037

ECO:0000322

imported manually asserted information used in automatic assertion

UniProtKB-KW:KW-0067

F

Seeded From UniProt

complete

part_of

GO:0016459

myosin complex

GO_REF:0000037

ECO:0000322

imported manually asserted information used in automatic assertion

UniProtKB-KW:KW-0518

C

Seeded From UniProt

complete

enables

GO:0000166

nucleotide binding

GO_REF:0000037

ECO:0000322

imported manually asserted information used in automatic assertion

UniProtKB-KW:KW-0547

F

Seeded From UniProt

complete

enables

GO:0003779

actin binding

GO_REF:0000037

ECO:0000322

imported manually asserted information used in automatic assertion

UniProtKB-KW:KW-0009

F

Seeded From UniProt

complete

enables

GO:0005516

calmodulin binding

GO_REF:0000037

ECO:0000322

imported manually asserted information used in automatic assertion

UniProtKB-KW:KW-0112

F

Seeded From UniProt

complete

part_of

GO:0005938

cell cortex

GO_REF:0000039

ECO:0000322

imported manually asserted information used in automatic assertion

UniProtKB-SubCell:SL-0138

C

Seeded From UniProt

complete

edit table

Notes

References

See Help:References for how to manage references in GONUTS.

  1. ↑ Huber, RJ & O'Day, DH (2015) Proteomic profiling of the extracellular matrix (slime sheath) of Dictyostelium discoideum. Proteomics 15 3315-9 PubMed GONUTS page
  2. ↑ Dharmawardhane, S et al. (1989) Changes in the association of actin-binding proteins with the actin cytoskeleton during chemotactic stimulation of Dictyostelium discoideum. Cell Motil. Cytoskeleton 13 57-63 PubMed GONUTS page
  3. ↑ Kee, YS et al. (2012) A mechanosensory system governs myosin II accumulation in dividing cells. Mol. Biol. Cell 23 1510-23 PubMed GONUTS page
  4. ↑ 4.0 4.1 Ogihara, S et al. (1988) Electron microscopic localization of myosin II and ABP-120 in the cortical actin matrix of Dictyostelium amoebae using IgG-gold conjugates. Dev. Genet. 9 505-20 PubMed GONUTS page
  5. ↑ 5.0 5.1 Pramanik, MK et al. (2009) PTEN is a mechanosensing signal transducer for myosin II localization in Dictyostelium cells. Genes Cells 14 821-34 PubMed GONUTS page
  6. ↑ Shelden, E & Knecht, DA (1996) Dictyostelium cell shape generation requires myosin II. Cell Motil. Cytoskeleton 35 59-67 PubMed GONUTS page
  7. ↑ Rosengarten, RD et al. (2015) Leaps and lulls in the developmental transcriptome of Dictyostelium discoideum. BMC Genomics 16 294 PubMed GONUTS page
  8. ↑ Srinivasan, K et al. (2013) Delineating the core regulatory elements crucial for directed cell migration by examining folic-acid-mediated responses. J. Cell. Sci. 126 221-33 PubMed GONUTS page
  9. ↑ Iwadate, Y et al. (2013) Myosin-II-mediated directional migration of Dictyostelium cells in response to cyclic stretching of substratum. Biophys. J. 104 748-58 PubMed GONUTS page
  10. ↑ Klein, JC et al. (2011) Structural and functional impact of site-directed methionine oxidation in myosin. Biochemistry 50 10318-27 PubMed GONUTS page
  11. ↑ Sugden, C et al. (2015) The Dictyostelium prestalk inducer differentiation-inducing factor-1 (DIF-1) triggers unexpectedly complex global phosphorylation changes. Mol. Biol. Cell 26 805-20 PubMed GONUTS page
  12. ↑ Müller-Taubenberger, A et al. (2002) Differential localization of the Dictyostelium kinase DPAKa during cytokinesis and cell migration. J. Muscle Res. Cell. Motil. 23 751-63 PubMed GONUTS page
  13. ↑ Zhou, Q et al. (2010) 14-3-3 coordinates microtubules, Rac, and myosin II to control cell mechanics and cytokinesis. Curr. Biol. 20 1881-9 PubMed GONUTS page
  14. ↑ 14.0 14.1 14.2 Iwadate, Y & Yumura, S (2008) Actin-based propulsive forces and myosin-II-based contractile forces in migrating Dictyostelium cells. J. Cell. Sci. 121 1314-24 PubMed GONUTS page
  15. ↑ 15.0 15.1 Gyimesi, M et al. (2008) Kinetic characterization of the function of myosin loop 4 in the actin-myosin interaction. Biochemistry 47 283-91 PubMed GONUTS page
  16. ↑ 16.0 16.1 16.2 16.3 Fujita-Becker, S et al. (2006) Functional characterization of the N-terminal region of myosin-2. J. Biol. Chem. 281 36102-9 PubMed GONUTS page
  17. ↑ Heid, PJ et al. (2005) Computer-assisted analysis of filopod formation and the role of myosin II heavy chain phosphorylation in Dictyostelium. J. Cell. Sci. 118 2225-37 PubMed GONUTS page
  18. ↑ Dickinson, DJ et al. (2012) α-catenin and IQGAP regulate myosin localization to control epithelial tube morphogenesis in Dictyostelium. Dev. Cell 23 533-46 PubMed GONUTS page
  19. ↑ Pasternak, C et al. (1989) Intermolecular versus intramolecular interactions of Dictyostelium myosin: possible regulation by heavy chain phosphorylation. J. Cell Biol. 109 203-10 PubMed GONUTS page
  20. ↑ 20.0 20.1 20.2 20.3 20.4 20.5 Clarke, M & Spudich, JA (1974) Biochemical and structural studies of actomyosin-like proteins from non-muscle cells. Isolation and characterization of myosin from amoebae of Dictyostelium discoideum. J. Mol. Biol. 86 209-22 PubMed GONUTS page
  21. ↑ 21.0 21.1 Betapudi, V & Egelhoff, TT (2009) Roles of an unconventional protein kinase and myosin II in amoeba osmotic shock responses. Traffic 10 1773-84 PubMed GONUTS page
  22. ↑ 22.0 22.1 22.2 Ito, K et al. (2009) Unique charge distribution in surface loops confers high velocity on the fast motor protein Chara myosin. Proc. Natl. Acad. Sci. U.S.A. 106 21585-90 PubMed GONUTS page
  23. ↑ Iwai, S et al. (2006) A point mutation in the SH1 helix alters elasticity and thermal stability of myosin II. J. Biol. Chem. 281 30736-44 PubMed GONUTS page
  24. ↑ 24.0 24.1 Moores, SL et al. (1996) Myosin dynamics in live Dictyostelium cells. Proc. Natl. Acad. Sci. U.S.A. 93 443-6 PubMed GONUTS page
  25. ↑ 25.0 25.1 Yoshida, K & Soldati, T (2006) Dissection of amoeboid movement into two mechanically distinct modes. J. Cell. Sci. 119 3833-44 PubMed GONUTS page
  26. ↑ Langridge, PD & Kay, RR (2006) Blebbing of Dictyostelium cells in response to chemoattractant. Exp. Cell Res. 312 2009-17 PubMed GONUTS page
  27. ↑ Dieckmann, R et al. (2010) A myosin IK-Abp1-PakB circuit acts as a switch to regulate phagocytosis efficiency. Mol. Biol. Cell 21 1505-18 PubMed GONUTS page
  28. ↑ Shu, S et al. (2012) Actin cross-linking proteins cortexillin I and II are required for cAMP signaling during Dictyostelium chemotaxis and development. Mol. Biol. Cell 23 390-400 PubMed GONUTS page
  29. ↑ 29.0 29.1 De Lozanne, A & Spudich, JA (1987) Disruption of the Dictyostelium myosin heavy chain gene by homologous recombination. Science 236 1086-91 PubMed GONUTS page
  30. ↑ 30.0 30.1 Manstein, DJ et al. (1989) Gene replacement in Dictyostelium: generation of myosin null mutants. EMBO J. 8 923-32 PubMed GONUTS page
  31. ↑ 31.0 31.1 Girard, KD et al. (2006) Dictyostelium myosin II mechanochemistry promotes active behavior of the cortex on long time scales. Proc. Natl. Acad. Sci. U.S.A. 103 2103-8 PubMed GONUTS page
  32. ↑ 32.0 32.1 Diez, S et al. (2005) Subsecond reorganization of the actin network in cell motility and chemotaxis. Proc. Natl. Acad. Sci. U.S.A. 102 7601-6 PubMed GONUTS page
  33. ↑ Clark, RJ et al. (2003) Probing nucleotide dissociation from myosin in vitro using microgram quantities of myosin. J. Muscle Res. Cell. Motil. 24 315-21 PubMed GONUTS page
  34. ↑ Chen, Q et al. (2006) Contractile ring-independent localization of DdINCENP, a protein important for spindle stability and cytokinesis. Mol. Biol. Cell 17 779-88 PubMed GONUTS page
  35. ↑ 35.0 35.1 Asano, Y et al. (2004) Keratocyte-like locomotion in amiB-null Dictyostelium cells. Cell Motil. Cytoskeleton 59 17-27 PubMed GONUTS page
  36. ↑ Reines, D & Clarke, M (1985) Quantitative immunochemical studies of myosin in Dictyostelium discoideum. J. Biol. Chem. 260 1133-40 PubMed GONUTS page
  37. ↑ Niswonger, ML & O'Halloran, TJ (1997) A novel role for clathrin in cytokinesis. Proc. Natl. Acad. Sci. U.S.A. 94 8575-8 PubMed GONUTS page
  38. ↑ Siddique, MS et al. (2005) Evidence against essential roles for subdomain 1 of actin in actomyosin sliding movements. Biochem. Biophys. Res. Commun. 332 474-81 PubMed GONUTS page
  39. ↑ Etzrodt, M et al. (2006) Time-resolved responses to chemoattractant, characteristic of the front and tail of Dictyostelium cells. FEBS Lett. 580 6707-13 PubMed GONUTS page
  40. ↑ 40.0 40.1 Nagasaki, A et al. (2009) Cell adhesion molecules regulate contractile ring-independent cytokinesis in Dictyostelium discoideum. Cell Res. 19 236-46 PubMed GONUTS page
  41. ↑ Kwak, E et al. (1999) LvsA, a protein related to the mouse beige protein, is required for cytokinesis in Dictyostelium. Mol. Biol. Cell 10 4429-39 PubMed GONUTS page
  42. ↑ Hostetter, D et al. (2004) Dictyostelium myosin bipolar thick filament formation: importance of charge and specific domains of the myosin rod. PLoS Biol. 2 e356 PubMed GONUTS page
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