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Article: The Cancer Testis Antigen Testis Specific Serine Kinase 6 (TSSK6) is abnormally expressed in colorectal cancer and promotes oncogenic behaviors.

Delgado, Magdalena / Gallegos, Zachary / McGlynn, Kathleen / Stippec, Steve / Cobb, Melanie H / Whitehurst, Angelique

bioRxiv : the preprint server for biology

2024

Abstract: Cancer testis antigens (CTAs) are a collection of proteins whose expression is normally restricted to the gamete, but abnormally activated in a wide variety of tumors. The CTA, Testis specific serine kinase 6 (TSSK6), is essential for male fertility in ... ...

Abstract	Cancer testis antigens (CTAs) are a collection of proteins whose expression is normally restricted to the gamete, but abnormally activated in a wide variety of tumors. The CTA, Testis specific serine kinase 6 (TSSK6), is essential for male fertility in mice. Functional relevance of TSSK6 to cancer, if any, has not previously been investigated. Here we find that TSSK6 is frequently anomalously expressed in colorectal cancer and patients with elevated TSSK6 expression have reduced relapse free survival. Depletion of TSSK6 from colorectal cancer cells attenuates anchorage independent growth, invasion and growth in vivo. Conversely, overexpression of TSSK6 enhances anchorage independence and invasion in vitro as well as in vivo tumor growth. Notably, ectopic expression of TSSK6 in semi-transformed human colonic epithelial cells is sufficient to confer anchorage independence and enhance invasion. In somatic cells, TSSK6 co-localizes with and enhances the formation of paxillin and tensin positive foci at the cell periphery, suggesting a function in focal adhesion formation. Importantly, TSSK6 kinase activity is essential to induce these tumorigenic behaviors. Our findings establish that TSSK6 exhibits oncogenic activity when abnormally expressed in colorectal cancer cells. Thus, TSSK6 is a previously unrecognized intervention target for therapy, which could exhibit an exceptionally broad therapeutic window.
Language	English
Publishing date	2024-04-30
Publishing country	United States
Document type	Preprint
DOI	10.1101/2024.01.08.574658
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Article ; Online: Testis Specific Serine Kinase 6 (TSSK6) is abnormally expressed in colorectal cancer and promotes oncogenic behaviors.

Delgado, Magdalena / Gallegos, Zachary / Stippec, Steve / McGlynn, Kathleen / Cobb, Melanie H / Whitehurst, Angelique W

The Journal of biological chemistry

2024 , Page(s) 107380

Abstract	Cancer testis antigens (CTAs) are a collection of proteins whose expression is normally restricted to the gamete, but abnormally activated in a wide variety of tumors. The CTA, Testis specific serine kinase 6 (TSSK6), is essential for male fertility in mice. Functional relevance of TSSK6 to cancer, if any, has not previously been investigated. Here we find that TSSK6 is frequently anomalously expressed in colorectal cancer and patients with elevated TSSK6 expression have reduced relapse free survival. Depletion of TSSK6 from colorectal cancer cells attenuates anchorage independent growth, invasion and growth in vivo. Conversely, overexpression of TSSK6 enhances anchorage independence and invasion in vitro as well as in vivo tumor growth. Notably, ectopic expression of TSSK6 in semi-transformed human colonic epithelial cells is sufficient to confer anchorage independence and enhance invasion. In somatic cells, TSSK6 co-localizes with and enhances the formation of paxillin and tensin positive foci at the cell periphery, suggesting a function in focal adhesion formation. Importantly, TSSK6 kinase activity is essential to induce these tumorigenic behaviors. Our findings establish that TSSK6 exhibits oncogenic activity when abnormally expressed in colorectal cancer cells. Thus, TSSK6 is a previously unrecognized intervention target for therapy, which could exhibit an exceptionally broad therapeutic window.
Language	English
Publishing date	2024-05-16
Publishing country	United States
Document type	Journal Article
ZDB-ID	2997-x
ISSN	1083-351X ; 0021-9258
ISSN (online)	1083-351X
ISSN	0021-9258
DOI	10.1016/j.jbc.2024.107380
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Article ; Online: ERK2 Mutations Affect Interactions, Localization, and Dimerization.

Taylor, Clinton A / Cormier, Kevin W / Martin-Vega, Ana / Earnest, Svetlana / Stippec, Steve / Wichaidit, Chonlarat / Cobb, Melanie H

Biochemistry

2023 Volume 62, Issue 9, Page(s) 1433–1442

Abstract: The most frequent ERK2 (MAPK1) mutation in cancers, E322K, lies in the common docking (CD) site, which binds short motifs made up of basic and hydrophobic residues present in the activators MEK1 (MAP2K1) and MEK2 (MAP2K2), in dual specificity ... ...

Abstract	The most frequent ERK2 (MAPK1) mutation in cancers, E322K, lies in the common docking (CD) site, which binds short motifs made up of basic and hydrophobic residues present in the activators MEK1 (MAP2K1) and MEK2 (MAP2K2), in dual specificity phosphatases (DUSPs) that inactivate the kinases, and in many of their substrates. Also, part of the CD site, but mutated less often in cancers, is the preceding aspartate (D321N). These mutants were categorized as gain of function in a sensitized melanoma system. In Drosophila developmental assays, we found that the aspartate but not the glutamate mutant caused gain-of-function phenotypes. Here, we catalogued additional properties of these mutants to accrue greater insight into their functions. A modest increase in nuclear retention of E322K was noted. Binding of ERK2 E322K and D321N to a small group of substrates and regulatory proteins was similar, in spite of differences in CD site integrity. Interactions with a second docking site, the F site, which should be more accessible in E322K, were modestly reduced rather than increased. The crystal structure of ERK2 E322K also indicated a disturbed dimer interface, and reduced dimerization was detected by a two-hybrid test; yet, it was detected in dimers in EGF-treated cells, although to a lesser extent than D321N or wt ERK2. These findings indicate a range of small differences in behaviors that may contribute to increased function of E322K in certain cancers.
MeSH term(s)	Animals ; Aspartic Acid ; Drosophila ; MAP Kinase Signaling System/physiology ; Mutation ; Phosphorylation ; Mitogen-Activated Protein Kinase 1/genetics ; Drosophila Proteins/genetics ; Protein Multimerization
Chemical Substances	Aspartic Acid (30KYC7MIAI) ; Mitogen-Activated Protein Kinase 1 (EC 2.7.11.24) ; Drosophila Proteins
Language	English
Publishing date	2023-04-06
Publishing country	United States
Document type	Journal Article ; Research Support, N.I.H., Extramural ; Research Support, Non-U.S. Gov't
ZDB-ID	1108-3
ISSN	1520-4995 ; 0006-2960
ISSN (online)	1520-4995
ISSN	0006-2960
DOI	10.1021/acs.biochem.3c00044
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Article ; Online: Mimicking Protein Kinase C Phosphorylation Inhibits Arc/Arg3.1 Palmitoylation and Its Interaction with Nucleic Acids.

Barylko, Barbara / Taylor, Clinton A / Wang, Jason / Earnest, Svetlana / Stippec, Steve / Binns, Derk D / Brautigam, Chad A / Jameson, David M / DeMartino, George N / Cobb, Melanie H / Albanesi, Joseph P

International journal of molecular sciences

2024 Volume 25, Issue 2

Abstract: Activity-regulated cytoskeleton-associated protein (Arc) plays essential roles in diverse forms of synaptic plasticity, including long-term potentiation (LTP), long-term depression (LTD), and homeostatic plasticity. In addition, it assembles into virus- ... ...

Abstract	Activity-regulated cytoskeleton-associated protein (Arc) plays essential roles in diverse forms of synaptic plasticity, including long-term potentiation (LTP), long-term depression (LTD), and homeostatic plasticity. In addition, it assembles into virus-like particles that may deliver mRNAs and/or other cargo between neurons and neighboring cells. Considering this broad range of activities, it is not surprising that Arc is subject to regulation by multiple types of post-translational modification, including phosphorylation, palmitoylation, SUMOylation, ubiquitylation, and acetylation. Here we explore the potential regulatory role of Arc phosphorylation by protein kinase C (PKC), which occurs on serines 84 and 90 within an α-helical segment in the N-terminal domain. To mimic the effect of PKC phosphorylation, we mutated the two serines to negatively charged glutamic acid. A consequence of introducing these phosphomimetic mutations is the almost complete inhibition of Arc palmitoylation, which occurs on nearby cysteines and contributes to synaptic weakening. The mutations also inhibit the binding of nucleic acids and destabilize high-order Arc oligomers. Thus, PKC phosphorylation of Arc may limit the full expression of LTD and may suppress the interneuronal transport of mRNAs.
MeSH term(s)	Phosphorylation ; Lipoylation ; Nucleic Acids ; Protein Processing, Post-Translational ; Protein Kinase C/genetics
Chemical Substances	Nucleic Acids ; Protein Kinase C (EC 2.7.11.13)
Language	English
Publishing date	2024-01-08
Publishing country	Switzerland
Document type	Journal Article
ZDB-ID	2019364-6
ISSN	1422-0067 ; 1422-0067 ; 1661-6596
ISSN (online)	1422-0067
ISSN	1422-0067 ; 1661-6596
DOI	10.3390/ijms25020780
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Article: Assaying protein kinase activity with radiolabeled atp

Karra, Aroon S / Stippec, Steve / Cobb, Melanie H

Journal of visualized experiments. 2017 May 26, , no. 123

2017

Abstract: Protein kinases are able to govern large-scale cellular changes in response to complex arrays of stimuli, and much effort has been directed at uncovering allosteric details of their regulation. Kinases comprise signaling networks whose defects are often ... ...

Abstract	Protein kinases are able to govern large-scale cellular changes in response to complex arrays of stimuli, and much effort has been directed at uncovering allosteric details of their regulation. Kinases comprise signaling networks whose defects are often hallmarks of multiple forms of cancer and related diseases, making an assay platform amenable to manipulation of upstream regulatory factors and validation of reaction requirements critical in the search for improved therapeutics. Here, we describe a basic kinase assay that can be easily adapted to suit specific experimental questions including but not limited to testing the effects of biochemical and pharmacological agents, genetic manipulations such as mutation and deletion, as well as cell culture conditions and treatments to probe cell signaling mechanisms. This assay utilizes radiolabeled [γ-32P] ATP, which allows for quantitative comparisons and clear visualization of results, and can be modified for use with immunoprecipitated or recombinant kinase, specific or typified substrates, all over a wide range of reaction conditions.
Keywords	adenosine triphosphate ; cell culture ; enzyme activity ; genetic engineering ; mutation ; neoplasms ; protein kinases ; radiolabeling ; therapeutics
Language	English
Dates of publication	2017-0526
Size	p. e55504.
Publishing place	Journal of Visualized Experiments
Document type	Article
ZDB-ID	2259946-0
ISSN	1940-087X
ISSN	1940-087X
DOI	10.3791/55504
Database	NAL-Catalogue (AGRICOLA)

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Article ; Online: Assaying Protein Kinase Activity with Radiolabeled ATP.

Karra, Aroon S / Stippec, Steve / Cobb, Melanie H

Journal of visualized experiments : JoVE

2017 , Issue 123

Abstract	Protein kinases are able to govern large-scale cellular changes in response to complex arrays of stimuli, and much effort has been directed at uncovering allosteric details of their regulation. Kinases comprise signaling networks whose defects are often hallmarks of multiple forms of cancer and related diseases, making an assay platform amenable to manipulation of upstream regulatory factors and validation of reaction requirements critical in the search for improved therapeutics. Here, we describe a basic kinase assay that can be easily adapted to suit specific experimental questions including but not limited to testing the effects of biochemical and pharmacological agents, genetic manipulations such as mutation and deletion, as well as cell culture conditions and treatments to probe cell signaling mechanisms. This assay utilizes radiolabeled [γ-
MeSH term(s)	Adenosine Triphosphate/metabolism ; Humans ; Phosphorus Radioisotopes/analysis ; Phosphorylation ; Protein Kinases/metabolism ; Radiopharmaceuticals/analysis ; Radiopharmaceuticals/metabolism ; Signal Transduction
Chemical Substances	Phosphorus Radioisotopes ; Radiopharmaceuticals ; Adenosine Triphosphate (8L70Q75FXE) ; Protein Kinases (EC 2.7.-)
Language	English
Publishing date	2017-05-26
Publishing country	United States
Document type	Journal Article ; Video-Audio Media ; Research Support, Non-U.S. Gov't ; Research Support, N.I.H., Extramural
ISSN	1940-087X
ISSN (online)	1940-087X
DOI	10.3791/55504
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Article ; Online: WNK1 is an unexpected autophagy inhibitor.

Gallolu Kankanamalage, Sachith / Lee, A-Young / Wichaidit, Chonlarat / Lorente-Rodriguez, Andres / Shah, Akansha M / Stippec, Steve / Whitehurst, Angelique W / Cobb, Melanie H

Autophagy

2017 Volume 13, Issue 5, Page(s) 969–970

Abstract: Autophagy is a cellular degradation pathway that is essential to maintain cellular physiology, and deregulation of autophagy leads to multiple diseases in humans. In a recent study, we discovered that the protein kinase WNK1 (WNK lysine deficient protein ...

Abstract	Autophagy is a cellular degradation pathway that is essential to maintain cellular physiology, and deregulation of autophagy leads to multiple diseases in humans. In a recent study, we discovered that the protein kinase WNK1 (WNK lysine deficient protein kinase 1) is an inhibitor of autophagy. The loss of WNK1 increases both basal and starvation-induced autophagy. In addition, the depletion of WNK1 increases the activation of the class III phosphatidylinositol 3-kinase (PtdIns3K) complex, which is required to induce autophagy. Moreover, the loss of WNK1 increases the expression of ULK1 (unc-51 like kinase 1), which is upstream of the PtdIns3K complex. It also increases the pro-autophagic phosphorylation of ULK1 at Ser555 and the activation of AMPK (AMP-activated protein kinase), which is responsible for that phosphorylation. The inhibition of AMPK by compound C decreases the magnitude of autophagy induction following WNK1 loss; however, it does not prevent autophagy induction. We found that the UVRAG (UV radiation resistance associated gene), which is a component of the PtdIns3K, binds to the N-terminal region of WNK1. Moreover, WNK1 partially colocalizes with UVRAG and this colocalization decreases when autophagy is stimulated in cells. The loss of WNK1 also alters the cellular distribution of UVRAG. The depletion of the downstream target of WNK1, OXSR1/OSR1 (oxidative-stress responsive 1) has no effect on autophagy, whereas the depletion of its relative STK39/SPAK (serine/threonine kinase 39) induces autophagy under nutrient-rich and starved conditions.
Language	English
Publishing date	2017-05-04
Publishing country	United States
Document type	Journal Article
ZDB-ID	2454135-7
ISSN	1554-8635 ; 1554-8627
ISSN (online)	1554-8635
ISSN	1554-8627
DOI	10.1080/15548627.2017.1286431
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Article ; Online: Functional divergence caused by mutations in an energetic hotspot in ERK2.

Taylor, Clinton A / Cormier, Kevin W / Keenan, Shannon E / Earnest, Svetlana / Stippec, Steve / Wichaidit, Chonlarat / Juang, Yu-Chi / Wang, Junmei / Shvartsman, Stanislav Y / Goldsmith, Elizabeth J / Cobb, Melanie H

Proceedings of the National Academy of Sciences of the United States of America

2019 Volume 116, Issue 31, Page(s) 15514–15523

Abstract: The most frequent extracellular signal-regulated kinase 2 (ERK2) mutation occurring in cancers is E322K (E-K). ERK2 E-K reverses a buried charge in the ERK2 common docking (CD) site, a region that binds activators, inhibitors, and substrates. Little is ... ...

Abstract	The most frequent extracellular signal-regulated kinase 2 (ERK2) mutation occurring in cancers is E322K (E-K). ERK2 E-K reverses a buried charge in the ERK2 common docking (CD) site, a region that binds activators, inhibitors, and substrates. Little is known about the cellular consequences associated with this mutation, other than apparent increases in tumor resistance to pathway inhibitors. ERK2 E-K, like the mutation of the preceding aspartate (ERK2 D321N [D-N]) known as the sevenmaker mutation, causes increased activity in cells and evades inactivation by dual-specificity phosphatases. As opposed to findings in cancer cells, in developmental assays in
MeSH term(s)	Animals ; Animals, Genetically Modified ; Crystallography, X-Ray ; Drosophila Proteins/chemistry ; Drosophila Proteins/genetics ; Drosophila Proteins/metabolism ; Drosophila melanogaster/enzymology ; Drosophila melanogaster/genetics ; Enzyme Activation ; Enzyme Stability ; Extracellular Signal-Regulated MAP Kinases/chemistry ; Extracellular Signal-Regulated MAP Kinases/genetics ; Extracellular Signal-Regulated MAP Kinases/metabolism ; Humans ; Models, Molecular ; Mutant Proteins/metabolism ; Mutation/genetics
Chemical Substances	Drosophila Proteins ; Mutant Proteins ; Extracellular Signal-Regulated MAP Kinases (EC 2.7.11.24) ; rl protein, Drosophila (EC 2.7.11.24)
Language	English
Publishing date	2019-07-11
Publishing country	United States
Document type	Journal Article ; Research Support, N.I.H., Extramural ; Research Support, Non-U.S. Gov't ; Research Support, U.S. Gov't, Non-P.H.S.
ZDB-ID	209104-5
ISSN	1091-6490 ; 0027-8424
ISSN (online)	1091-6490
ISSN	0027-8424
DOI	10.1073/pnas.1905015116
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Article ; Online: Multistep regulation of autophagy by WNK1.

Gallolu Kankanamalage, Sachith / Lee, A-Young / Wichaidit, Chonlarat / Lorente-Rodriguez, Andres / Shah, Akansha M / Stippec, Steve / Whitehurst, Angelique W / Cobb, Melanie H

Proceedings of the National Academy of Sciences of the United States of America

2016 Volume 113, Issue 50, Page(s) 14342–14347

Abstract: The with-no-lysine (K) (WNK) kinases are an atypical family of protein kinases that regulate ion transport across cell membranes. Mutations that result in their overexpression cause hypertension-related disorders in humans. Of the four mammalian WNKs, ... ...

Abstract	The with-no-lysine (K) (WNK) kinases are an atypical family of protein kinases that regulate ion transport across cell membranes. Mutations that result in their overexpression cause hypertension-related disorders in humans. Of the four mammalian WNKs, only WNK1 is expressed throughout the body. We report that WNK1 inhibits autophagy, an intracellular degradation pathway implicated in several human diseases. Using small-interfering RNA-mediated WNK1 knockdown, we show autophagosome formation and autophagic flux are accelerated. In cells with reduced WNK1, basal and starvation-induced autophagy is increased. We also show that depletion of WNK1 stimulates focal class III phosphatidylinositol 3-kinase complex (PI3KC3) activity, which is required to induce autophagy. Depletion of WNK1 increases the expression of the PI3KC3 upstream regulator unc-51-like kinase 1 (ULK1), its phosphorylation, and activation of the kinase upstream of ULK1, the AMP-activated protein kinase. In addition, we show that the N-terminal region of WNK1 binds to the UV radiation resistance-associated gene (UVRAG) in vitro and WNK1 partially colocalizes with UVRAG, a component of a PI3KC3 complex. This colocalization decreases upon starvation of cells. Depletion of the SPS/STE20-related proline-alanine-rich kinase, a WNK1-activated enzyme, also induces autophagy in nutrient-replete or -starved conditions, but depletion of the related kinase and WNK1 substrate, oxidative stress responsive 1, does not. These results indicate that WNK1 inhibits autophagy by multiple mechanisms.
MeSH term(s)	Autophagy/genetics ; Autophagy/physiology ; Autophagy-Related Protein-1 Homolog/metabolism ; Cell Line ; Class III Phosphatidylinositol 3-Kinases/metabolism ; Gene Knockdown Techniques ; HeLa Cells ; Humans ; Intracellular Signaling Peptides and Proteins/metabolism ; Models, Biological ; Protein-Serine-Threonine Kinases/antagonists & inhibitors ; Protein-Serine-Threonine Kinases/genetics ; Protein-Serine-Threonine Kinases/metabolism ; RNA, Small Interfering/genetics ; Tumor Suppressor Proteins/genetics ; Tumor Suppressor Proteins/metabolism ; WNK Lysine-Deficient Protein Kinase 1/antagonists & inhibitors ; WNK Lysine-Deficient Protein Kinase 1/genetics ; WNK Lysine-Deficient Protein Kinase 1/physiology
Chemical Substances	Intracellular Signaling Peptides and Proteins ; RNA, Small Interfering ; Tumor Suppressor Proteins ; UVRAG protein, human ; OXSR1 protein, human (EC 2.7.1.-) ; Class III Phosphatidylinositol 3-Kinases (EC 2.7.1.137) ; Autophagy-Related Protein-1 Homolog (EC 2.7.11.1) ; Protein-Serine-Threonine Kinases (EC 2.7.11.1) ; STK39 protein, human (EC 2.7.11.1) ; ULK1 protein, human (EC 2.7.11.1) ; WNK Lysine-Deficient Protein Kinase 1 (EC 2.7.11.1) ; WNK1 protein, human (EC 2.7.11.1)
Language	English
Publishing date	2016-11-28
Publishing country	United States
Document type	Journal Article ; Research Support, N.I.H., Extramural ; Research Support, Non-U.S. Gov't
ZDB-ID	209104-5
ISSN	1091-6490 ; 0027-8424
ISSN (online)	1091-6490
ISSN	0027-8424
DOI	10.1073/pnas.1617649113
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Article ; Online: OSR1 regulates a subset of inward rectifier potassium channels via a binding motif variant.

Taylor, Clinton A / An, Sung-Wan / Kankanamalage, Sachith Gallolu / Stippec, Steve / Earnest, Svetlana / Trivedi, Ashesh T / Yang, Jonathan Zijiang / Mirzaei, Hamid / Huang, Chou-Long / Cobb, Melanie H

Proceedings of the National Academy of Sciences of the United States of America

2018 Volume 115, Issue 15, Page(s) 3840–3845

Abstract: The with-no-lysine (K) (WNK) signaling pathway to STE20/SPS1-related proline- and alanine-rich kinase (SPAK) and oxidative stress-responsive 1 (OSR1) kinase is an important mediator of cell volume and ion transport. SPAK and OSR1 associate with upstream ... ...

Abstract	The with-no-lysine (K) (WNK) signaling pathway to STE20/SPS1-related proline- and alanine-rich kinase (SPAK) and oxidative stress-responsive 1 (OSR1) kinase is an important mediator of cell volume and ion transport. SPAK and OSR1 associate with upstream kinases WNK 1-4, substrates, and other proteins through their C-terminal domains which interact with linear R-F-x-V/I sequence motifs. In this study we find that SPAK and OSR1 also interact with similar affinity with a motif variant, R-x-F-x-V/I. Eight of 16 human inward rectifier K
MeSH term(s)	Amino Acid Motifs ; Amino Acid Sequence ; Humans ; Molecular Sequence Data ; Multigene Family ; Mutation ; Potassium Channels, Inwardly Rectifying/chemistry ; Potassium Channels, Inwardly Rectifying/genetics ; Potassium Channels, Inwardly Rectifying/metabolism ; Protein Domains ; Protein-Serine-Threonine Kinases/genetics ; Protein-Serine-Threonine Kinases/metabolism ; Sequence Alignment ; Signal Transduction
Chemical Substances	Kir2.1 channel ; Kir2.2 channel ; Potassium Channels, Inwardly Rectifying ; OXSR1 protein, human (EC 2.7.1.-) ; Protein-Serine-Threonine Kinases (EC 2.7.11.1) ; STK39 protein, human (EC 2.7.11.1)
Language	English
Publishing date	2018-03-26
Publishing country	United States
Document type	Journal Article ; Research Support, N.I.H., Extramural ; Research Support, Non-U.S. Gov't
ZDB-ID	209104-5
ISSN	1091-6490 ; 0027-8424
ISSN (online)	1091-6490
ISSN	0027-8424
DOI	10.1073/pnas.1802339115
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