scholarly journals Dictyostelium discoideum has a single diacylglycerol kinase gene with similarity to mammalian θ isoforms

2002 ◽  
Vol 368 (3) ◽  
pp. 809-815 ◽  
Author(s):  
Marc A. de la ROCHE ◽  
Janet L. SMITH ◽  
Maribel RICO ◽  
Silvia CARRASCO ◽  
Isabel MERIDA ◽  
...  
Keyword(s):  
Protein Kinase ◽  
Dictyostelium Discoideum ◽  
Heavy Chain ◽  
Catalytic Domain ◽  
Single Gene ◽  
Myosin Ii ◽  
Terminal Segment ◽  
Gene Encoding ◽  
Kinase Gene ◽  
Myosin Heavy Chain Protein

Diacylglycerol kinases (DGKs) phosphorylate the neutral lipid diacylglycerol (DG) to produce phosphatidic acid (PA). In mammalian systems DGKs are a complex family of at least nine isoforms that are thought to participate in down-regulation of DG-based signalling pathways and perhaps activation of PA-stimulated signalling events. We report here that the simple protozoan amoeba Dictyostelium discoideum appears to contain a single gene encoding a DGK enzyme. This gene, dgkA, encodes a deduced protein that contains three C1-type cysteine-rich repeats, a DGK catalytic domain most closely related to the θ subtype of mammalian DGKs and a C-terminal segment containing a proline/glutamine-rich region and a large aspargine-repeat region. This gene corresponds to a previously reported myosin II heavy chain kinase designated myosin heavy chain-protein kinase C (MHC-PKC), but our analysis clearly demonstrates that this protein does not, as suggested by earlier data, contain a protein kinase catalytic domain. A FLAG-tagged version of DgkA expressed in Dictyostelium displayed robust DGK activity. Earlier studies indicating that disruption of this locus alters myosin II assembly levels in Dictyostelium raise the intriguing possibility that DG and/or PA metabolism may play a role in controlling myosin II assembly in this system.

scholarly journals Mapping of the Novel Protein Kinase Catalytic Domain ofDictyosteliumMyosin II Heavy Chain Kinase A

1997 ◽  
Vol 272 (11) ◽  
pp. 6846-6849 ◽  
Author(s):  
Graham P. Côté ◽  
Xia Luo ◽  
Michael B. Murphy ◽  
Thomas T. Egelhoff
Keyword(s):  
Protein Kinase ◽  
Heavy Chain ◽  
Catalytic Domain ◽  
The Novel ◽  
Kinase Catalytic Domain ◽  
Kinase A ◽  
Novel Protein

scholarly journals Ciliopathy-Associated Protein Kinase ICK Requires Its Non-Catalytic Carboxyl-Terminal Domain for Regulation of Ciliogenesis

Cells ◽  
2019 ◽  
Vol 8 (7) ◽  
pp. 677 ◽  
Author(s):  
Yoon Seon Oh ◽  
Eric J. Wang ◽  
Casey D. Gailey ◽  
David L. Brautigan ◽  
Benjamin L. Allen ◽  
...  
Keyword(s):  
Protein Kinase ◽  
Primary Cilia ◽  
Catalytic Domain ◽  
Intestinal Cell ◽  
Loss Of Function ◽  
Kinase Gene ◽  
Intrinsically Disordered ◽  
Terminal Domain ◽  
Perinatal Lethality ◽  
Carboxyl Terminal

Loss-of-function mutations in the human ICK (intestinal cell kinase) gene cause dysfunctional primary cilia and perinatal lethality which are associated with human ciliopathies. The enzyme that we herein call CAPK (ciliopathy-associated protein kinase) is a serine/threonine protein kinase that has a highly conserved MAPK-like N-terminal catalytic domain and an unstructured C-terminal domain (CTD) whose functions are completely unknown. In this study, we demonstrate that truncation of the CTD impairs the ability of CAPK to interact with and phosphorylate its substrate, kinesin family member 3A (KIF3A). We also find that deletion of the CTD of CAPK compromises both localization to the primary cilium and negative regulation of ciliogenesis. Thus, CAPK substrate recognition, ciliary targeting, and ciliary function depend on the non-catalytic CTD of the protein which is predicted to be intrinsically disordered.

scholarly journals byr2, a Schizosaccharomyces pombe gene encoding a protein kinase capable of partial suppression of the ras1 mutant phenotype.

1991 ◽  
Vol 11 (7) ◽  
pp. 3554-3563 ◽  
Author(s):  
Y Wang ◽  
H P Xu ◽  
M Riggs ◽  
L Rodgers ◽  
M Wigler
Keyword(s):  
Protein Kinase ◽  
Schizosaccharomyces Pombe ◽  
Cell Shape ◽  
Single Gene ◽  
Gene Encoding ◽  
Ras Genes ◽  
Mutant Strains ◽  
Site Of Action ◽  
Partial Suppression ◽  
Normal Shape

Schizosaccharomyces pombe contains a single gene, ras1, which is a homolog of the mammalian RAS genes. ras1 is required for conjugation, sporulation, and normal cell shape. ras1 has been previously identified as ste5. We report here a gene we call byr2 that can encode a predicted protein kinase and can partially suppress defects in ras1 mutants. ras1 mutant strains expressing high levels of byr2 can sporulate competently but are still defective in conjugation and abnormally round. byr2 mutants are viable and have normal shape but are absolutely defective in conjugation and sporulation. byr2 is probably identical to ste8. In many respects, byr2 resembles the byr1 gene, another suppressor of the ras1 mutation, which has been identified previously as ste1. Our data indicate that if ras1, byr2, and byr1 act along the same pathway, then the site of action for byr2 is between the sites for ras1 and byr1.

scholarly journals byr2, a Schizosaccharomyces pombe gene encoding a protein kinase capable of partial suppression of the ras1 mutant phenotype

1991 ◽  
Vol 11 (7) ◽  
pp. 3554-3563 ◽  
Author(s):  
Y Wang ◽  
H P Xu ◽  
M Riggs ◽  
L Rodgers ◽  
M Wigler
Keyword(s):  
Protein Kinase ◽  
Schizosaccharomyces Pombe ◽  
Cell Shape ◽  
Single Gene ◽  
Gene Encoding ◽  
Ras Genes ◽  
Mutant Strains ◽  
Site Of Action ◽  
Partial Suppression ◽  
Normal Shape

Schizosaccharomyces pombe contains a single gene, ras1, which is a homolog of the mammalian RAS genes. ras1 is required for conjugation, sporulation, and normal cell shape. ras1 has been previously identified as ste5. We report here a gene we call byr2 that can encode a predicted protein kinase and can partially suppress defects in ras1 mutants. ras1 mutant strains expressing high levels of byr2 can sporulate competently but are still defective in conjugation and abnormally round. byr2 mutants are viable and have normal shape but are absolutely defective in conjugation and sporulation. byr2 is probably identical to ste8. In many respects, byr2 resembles the byr1 gene, another suppressor of the ras1 mutation, which has been identified previously as ste1. Our data indicate that if ras1, byr2, and byr1 act along the same pathway, then the site of action for byr2 is between the sites for ras1 and byr1.

scholarly journals Identification of a Protein Kinase fromDictyosteliumwith Homology to the Novel Catalytic Domain of Myosin Heavy Chain Kinase A

1997 ◽  
Vol 272 (18) ◽  
pp. 11812-11815 ◽  
Author(s):  
Colleen E. Clancy ◽  
Manual G. Mendoza ◽  
Teresa V. Naismith ◽  
Michael F. Kolman ◽  
Thomas T. Egelhoff
Keyword(s):  
Protein Kinase ◽  
Myosin Heavy Chain ◽  
Heavy Chain ◽  
Catalytic Domain ◽  
The Novel ◽  
Myosin Heavy Chain Kinase ◽  
Kinase A

scholarly journals Myosin‑II heavy chain and formin mediate the targeting of myosin essential light chain to the division site before and during cytokinesis

2015 ◽  
Vol 26 (7) ◽  
pp. 1211-1224 ◽  
Author(s):  
Zhonghui Feng ◽  
Satoshi Okada ◽  
Guoping Cai ◽  
Bing Zhou ◽  
Erfei Bi
Keyword(s):  
Heavy Chain ◽  
Light Chain ◽  
Membrane Trafficking ◽  
Myosin Ii ◽  
Myosin V ◽  
Gene Encoding ◽  
Yeast Saccharomyces Cerevisiae ◽  
Essential Light Chain ◽  
Division Site ◽  
Yeast Mutants

MLC1 is a haploinsufficient gene encoding the essential light chain for Myo1, the sole myosin‑II heavy chain in the budding yeast Saccharomyces cerevisiae. Mlc1 defines an essential hub that coordinates actomyosin ring function, membrane trafficking, and septum formation during cytokinesis by binding to IQGAP, myosin‑II, and myosin‑V. However, the mechanism of how Mlc1 is targeted to the division site during the cell cycle remains unsolved. By constructing a GFP‑tagged MLC1 under its own promoter control and using quantitative live‑cell imaging coupled with yeast mutants, we found that septin ring and actin filaments mediate the targeting of Mlc1 to the division site before and during cytokinesis, respectively. Both mechanisms contribute to and are collectively required for the accumulation of Mlc1 at the division site during cytokinesis. We also found that Myo1 plays a major role in the septin‑dependent Mlc1 localization before cytokinesis, whereas the formin Bni1 plays a major role in the actin filament–dependent Mlc1 localization during cytokinesis. Such a two‑tiered mechanism for Mlc1 localization is presumably required for the ordered assembly and robustness of cytokinesis machinery and is likely conserved across species.

Structural abnormalities develop in the brain after ablation of the gene encoding nonmuscle myosin II-B heavy chain

2001 ◽  
Vol 433 (1) ◽  
pp. 62-74 ◽  
Author(s):  
Antonella N. Tullio ◽  
Paul C. Bridgman ◽  
Nancy J. Tresser ◽  
Chi-Chao Chan ◽  
Mary Anne Conti ◽  
...  
Keyword(s):  
Heavy Chain ◽  
Myosin Ii ◽  
Nonmuscle Myosin ◽  
Gene Encoding ◽  
Nonmuscle Myosin Ii ◽  
Structural Abnormalities ◽  
The Brain

scholarly journals Dictyostelium myosin heavy chain kinase A regulates myosin localization during growth and development.

1996 ◽  
Vol 132 (1) ◽  
pp. 101-109 ◽  
Author(s):  
M F Kolman ◽  
L M Futey ◽  
T T Egelhoff
Keyword(s):  
Heavy Chain ◽  
Kinase Activity ◽  
Developmental Stages ◽  
Catalytic Domain ◽  
Myosin Ii ◽  
Significant Similarity ◽  
Dictyostelium Myosin ◽  
A Cells

Phosphorylation of the Dictyostelium myosin II heavy chain (MHC) has a key role in regulating myosin localization in vivo and drives filament disassembly in vitro. Previous molecular analysis of the Dictyostelium myosin II heavy chain kinase (MHCK A) gene has demonstrated that the catalytic domain of this enzyme is extremely novel, showing no significant similarity to the known classes of protein kinases (Futey, L. M., Q. G. Medley, G. P. Côté, and T. T. Egelhoff. 1995. J. Biol. Chem. 270:523-529). To address the physiological roles of this enzyme, we have analyzed the cellular consequences of MHCK A gene disruption (mhck A- cells) and MHCK A overexpression (MHCK A++ cells). The mhck A- cells are viable and competent for tested myosin-based contractile events, but display partial defects in myosin localization. Both growth phase and developed mhck A- cells show substantially reduced MHC kinase activity in crude lysates, as well as significant overassembly of myosin into the Triton-resistant cytoskeletal fractions. MHCK A++ cells display elevated levels of MHC kinase activity in crude extracts, and show reduced assembly of myosin into Triton-resistant cytoskeletal fractions. MHCK A++ cells show reduced growth rates in suspension, becoming large and multinucleated, and arrest at the mound stage during development. These results demonstrate that MHCK A functions in vivo as a protein kinase with physiological roles in regulating myosin II localization and assembly in Dictyostelium cells during both growth and developmental stages.

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